Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 1.16.3.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.16.3.1

Enzymes and Genes:
multicopper oxidase with role in copper homeostasis Inferred from experiment : cueO ( Escherichia coli K-12 substr. MG1655 )
ceruloplasmin Inferred from experiment : CP ( Homo sapiens )

Reaction Locations: periplasmic space (sensu Gram-negative Bacteria), cytosol

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: ferroxidase

Enzyme Commission Synonyms: ceruloplasmin, caeruloplasmin, ferroxidase I, iron oxidase, iron(II):oxygen oxidoreductase, ferro:O2 oxidoreductase, iron II:oxygen oxidoreductase, hephaestin, HEPH

Standard Gibbs Free Energy (ΔrG in kcal/mol): -13.166946 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.

Citations: [Osaki66, Osaki67, Chen04, Takai01]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R00078 , Rhea:11148

Relationship Links: BRENDA:EC:1.16.3.1 , ENZYME:EC:1.16.3.1 , IUBMB-ExplorEnz:EC:1.16.3.1 , UniProt:RELATED-TO:P00450

Credits:
Revised 01-Sep-2010 by Caspi R , SRI International


References

Chen04: Chen H, Attieh ZK, Su T, Syed BA, Gao H, Alaeddine RM, Fox TC, Usta J, Naylor CE, Evans RW, McKie AT, Anderson GJ, Vulpe CD (2004). "Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice." Blood 103(10);3933-9. PMID: 14751926

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Osaki66: Osaki S (1966). "Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin)." J Biol Chem 241(21);5053-9. PMID: 5925868

Osaki67: Osaki S, Walaas O (1967). "Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase. II. Rate constants at various steps and formation of a possible enzyme-substrate complex." J Biol Chem 242(11);2653-7. PMID: 6027241

Takai01: Takai M, Kamimura K, Sugio T (2001). "A new iron oxidase from a moderately thermophilic iron oxidizing bacterium strain TI-1." Eur J Biochem 268(6);1653-8. PMID: 11248684


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13B.