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Record Information
Version1.0
Creation Date2016-09-30 22:34:24 UTC
Update Date2020-05-11 22:28:19 UTC
BMDB IDBMDB0000657
Secondary Accession Numbers
  • BMDB00657
Metabolite Identification
Common NameCopper
DescriptionCopper, also known as cu(ii) or copper (ii) ion, belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom. Copper exists as a solid, possibly soluble (in water), and possibly neutral molecule. Copper exists in all living species, ranging from bacteria to humans. In cattle, copper is involved in the metabolic pathway called the tyrosine metabolism pathway. Copper is a potentially toxic compound. Copper has been found to be associated with several diseases known as aceruloplasminemia, mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma, and alzheimer's disease; also copper has been linked to several inborn metabolic disorders including hyperzincaemia and hypercalprotectinaemia and menkes disease.
Structure
Thumb
Synonyms
ValueSource
COPPER (II) ionChEBI
Copper(II) cationChEBI
Copper, ion (cu2+)ChEBI
Cu(II)ChEBI
Cu2+ChEBI
Cu(2+)ChEBI
Cupric ionChEBI
CuHMDB
Chemical FormulaCu
Average Molecular Weight63.546
Monoisotopic Molecular Weight62.929601079
IUPAC Namecopper(2+) ion
Traditional Namecopper(2+) ion
CAS Registry Number7440-50-8
SMILES
[Cu++]
InChI Identifier
InChI=1S/Cu/q+2
InChI KeyJPVYNHNXODAKFH-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Ontology
StatusDetected and Quantified
Origin
  • Exogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locations
  • Cytoplasm
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point1083 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP0.16ChemAxon
pKa (Strongest Acidic)3.09ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-9000000000-59c652eccc13cc365f65View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-03di-9000000000-59c652eccc13cc365f65View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-03di-9000000000-59c652eccc13cc365f65View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-9000000000-9acd78ab9faeb89677a7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-03di-9000000000-9acd78ab9faeb89677a7View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-03di-9000000000-9acd78ab9faeb89677a7View in MoNA
Biological Properties
Cellular Locations
  • Cytoplasm
Biospecimen Locations
  • Blood
  • Brain
  • Erythrocyte
  • Hair
  • Intestine
  • Kidney
  • Liver
  • Longissimus Thoracis Muscle
  • Milk
  • Ruminal Fluid
  • Semimembranosus Muscle
  • Testis
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified14.950 +/- 3.462 uMNot SpecifiedNot Specified
Normal
    • C. R. E. Cogginsa...
details
BloodDetected and Quantified9+/-2 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
BrainExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
ErythrocyteExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
HairExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
IntestineExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
KidneyExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
LiverDetected and Quantified27+/-19 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Longissimus Thoracis MuscleDetected and Quantified0.25+/-0.13 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
MilkDetected and Quantified1.416 uMNot SpecifiedNot Specified
Normal
    • NRC. 1989. Recomm...
details
MilkDetected and Quantified1.58 uM4-12 years oldNot SpecifiedNormal
    • Z. Dobrzañski et ...
details
MilkDetected and Quantified9.442 uMNot SpecifiedNot SpecifiedNormal
    • Park, Y. W; Juáre...
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.574 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified0.57 +/- 0.23 uMNot SpecifiedNot SpecifiedNormal
    • A. PECHOVÁ et al....
details
MilkDetected and Quantified1.1 +/- 0.1 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.4 +/- 0.2 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified1.3 +/- 0.1 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified2 +/- 1 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.0572 +/- 0.0944 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified1.401 +/- 0.0472 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified8.875 +/- 0.126 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified1.212 +/- 0.0944 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified2.0772 +/- 0.346 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified0.567 +/- 0.0944 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified1.259 - 1.731 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1.574 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1.259 - 8.498 uMNot SpecifiedNot SpecifiedNormal
    • Semaghiul Birghil...
details
MilkDetected and Quantified0.976 +/- 0.0787 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1.0229 - 1.401 uMNot SpecifiedNot SpecifiedNormal
    • Z. Dobrzański, R....
details
Ruminal FluidDetected and Quantified2.59 +/- 0.5 uMNot SpecifiedNot Specified
Normal
    • Fozia Saleem, Sou...
details
Ruminal FluidDetected and Quantified5+/-1 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Semimembranosus MuscleDetected and Quantified0.2+/-0.1 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
TestisDetected and Quantified0.7+/-0.1 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected but not QuantifiedNot ApplicableNot SpecifiedNot Specified
Fatal bovine respiratory disease
details
HMDB IDHMDB0000657
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB030749
KNApSAcK IDNot Available
Chemspider ID25221
KEGG Compound IDC00070
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkCopper
METLIN IDNot Available
PubChem Compound27099
PDB IDNot Available
ChEBI ID29036
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Campillo N, Vinas P, Lopez-Garcia I, Hernandez-Cordoba M: Direct determination of copper and zinc in cow milk, human milk and infant formula samples using electrothermal atomization atomic absorption spectrometry. Talanta. 1998 Aug;46(4):615-22. [PubMed:18967184 ]
  2. Gaucheron F: Milk and dairy products: a unique micronutrient combination. J Am Coll Nutr. 2011 Oct;30(5 Suppl 1):400S-9S. [PubMed:22081685 ]
  3. A. Pechová, L. Pavlata, R. Dvořák, E. Lokajová (2008). A. PECHOVÁ et al. Contents of Zn, Cu, Mn and Se in Milk in Relation to their Concentrations in Blood, Milk Yield and Stage of Lactation in Dairy Cattle. Acta Vet. Brno 2008, 77: 523-531. Acta Vet. Brno.
  4. NA (1989). NRC. 1989. Recommended Dietary Allowances. 10th ed. Natl. Acad. Press, Washington, DC.. The National Academies Press.
  5. Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu (2008). Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu. Determination of major and minor elements in milk through ICP-AES. Environmental Engineering and Management Journal. November/December 2008, Vol.7, No.6, 805-808. Environmental Engineering and Management Journal.
  6. Z. Dobrzañski, R. Ko3acz, H. Górecka, K. Chojnacka, A. Bartkowiak (2005). Z. Dobrzañski et al. The Content of Microelements and Trace Elements in Raw Milk from Cows in the Silesian Region. Polish Journal of Environmental Studies Vol. 14, No 5 (2005), 685-689. Polish Journal of Environmental Studies .
  7. Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. (2005). Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. 2005. The Content of Microelements and Trace Elements in Raw Milk from Cows in the Silesian Region. Pol. J. Environ. Stud. 14(5):685–689. Polish Journal of Environmental Studies.
  8. Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W. (2007). Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W.. Physico-chemical characteristics of goat and sheep milk. Small Ruminant Res.(2007) 68:88-113 doi: 10.1016/j.smallrumres.2006.09.013. Small Ruminant Research.
  9. A. Foroutan et al. (2019). A. Foroutan et al. The Chemical Composition of Commercial Cow's Milk (in preparation). Journal of Agricultural and Food Chemistry.
  10. Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia (2005). Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia. 2005. Room temperature acid sonication ICP-MS multielemental analysis of milk.Analytica Chimica Acta Volume 531, Issue 1, Pages 111-123. Analytica Chimica Acta.
  11. Fooddata+, The Technical University of Denmark (DTU) [Link]

Only showing the first 50 proteins. There are 60 proteins in total.

Enzymes

General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
MT-CO2
Uniprot ID:
P68530
Molecular weight:
26021.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
MT-CO1
Uniprot ID:
P00396
Molecular weight:
57032.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
Q45LD5
Molecular weight:
57086.0
General function:
Energy production and conversion
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
Q862S6
Molecular weight:
6166.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX2
Uniprot ID:
B1P072
Molecular weight:
25987.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
Not Available
Uniprot ID:
Q5BP91
Molecular weight:
21945.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMV6
Molecular weight:
20164.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMT7
Molecular weight:
20837.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMS5
Molecular weight:
21961.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
Q6QTG9
Molecular weight:
57035.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX2
Uniprot ID:
Q8M444
Molecular weight:
26020.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMS1
Molecular weight:
22058.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
Q7JAT4
Molecular weight:
57032.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
Q45LE8
Molecular weight:
57060.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
C5IS82
Molecular weight:
25404.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YN12
Molecular weight:
19067.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
Not Available
Uniprot ID:
A1XEF2
Molecular weight:
16763.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
Q45LN9
Molecular weight:
57002.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COII
Uniprot ID:
Q7JAT3
Molecular weight:
26021.0
General function:
Energy production and conversion
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
Q85E88
Molecular weight:
8407.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
C5IS85
Molecular weight:
25438.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YN01
Molecular weight:
19520.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX2
Uniprot ID:
Q3L5W1
Molecular weight:
26052.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMR7
Molecular weight:
22171.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COII
Uniprot ID:
B2KPB9
Molecular weight:
22251.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMW7
Molecular weight:
19834.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
A1XP62
Molecular weight:
8746.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
B1NZU1
Molecular weight:
57018.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
Q29437
Molecular weight:
84757.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity (By similarity).
Gene Name:
AOC3
Uniprot ID:
Q9TTK6
Molecular weight:
84500.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
O46406
Molecular weight:
84883.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
AOC1
Uniprot ID:
Q3MHQ1
Molecular weight:
85533.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
SOD1
Uniprot ID:
A4URH1
Molecular weight:
10512.0
General function:
Inorganic ion transport and metabolism
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene Name:
ECSOD
Uniprot ID:
A3KLR9
Molecular weight:
26177.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
Q861T4
Molecular weight:
12926.0
General function:
Inorganic ion transport and metabolism
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene Name:
SOD1
Uniprot ID:
P00442
Molecular weight:
15683.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
Q9TS96
Molecular weight:
11344.0
General function:
Involved in copper ion binding
Specific function:
Conversion of dopamine to noradrenaline.
Gene Name:
DBH
Uniprot ID:
P15101
Molecular weight:
68141.0
General function:
Energy production and conversion
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
A1XEF0
Molecular weight:
8325.0
General function:
Energy production and conversion
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
A1XEE6
Molecular weight:
8261.0
General function:
Involved in copper ion binding
Specific function:
Active on elastin and collagen substrates.
Gene Name:
LOXL1
Uniprot ID:
Q95L39
Molecular weight:
64496.0
General function:
Involved in copper ion binding
Specific function:
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity).
Gene Name:
LOX
Uniprot ID:
P33072
Molecular weight:
47115.0
General function:
Involved in copper ion binding
Specific function:
May modulate the formation of a collagenous extracellular matrix.
Gene Name:
LOXL4
Uniprot ID:
Q8MJ24
Molecular weight:
84050.0
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Gene Name:
COX11
Uniprot ID:
A3KMZ6
Molecular weight:
31824.0
General function:
Involved in copper ion binding
Specific function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone.
Gene Name:
TYR
Uniprot ID:
Q8MIU0
Molecular weight:
60304.0
General function:
Energy production and conversion
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
A1XEE9
Molecular weight:
8048.0
General function:
Involved in copper ion binding
Specific function:
Plays a role in melanin biosynthesis. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Also to a lower extent, capable of hydroxylating tyrosine and producing melanin.
Gene Name:
TYRP1
Uniprot ID:
Q8WN57
Molecular weight:
60617.0
General function:
Involved in copper ion binding
Specific function:
Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:2059626). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:2059626). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:2059626). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Gene Name:
PAM
Uniprot ID:
P10731
Molecular weight:
108177.0
General function:
Involved in copper ion binding
Specific function:
Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (PubMed:22677715). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017).
Gene Name:
ALB
Uniprot ID:
P02769
Molecular weight:
69293.0
General function:
Not Available
Specific function:
Required for nuclear and mitochondrial iron-sulfur protein biosynthesis.
Gene Name:
LYRM4
Uniprot ID:
Q0VCG0
Molecular weight:
10711.0

Only showing the first 50 proteins. There are 60 proteins in total.