|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 126.96.36.199
Enzymes and Genes:
|Homo sapiens :||methionine synthase reductase
Supersedes EC number: 188.8.131.52
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: Balance undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: [methionine synthase] reductase
Enzyme Commission Synonyms: methionine synthase cob(II)alamin reductase (methylating), methionine synthase reductase, [methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing)
Taxonomic Range: Metazoa
Enzyme Commission Summary:
In humans, the enzyme is a flavoprotein containing FAD and FMN. The substrate of the enzyme is the inactivated [Co(II)] form of EC 184.108.40.206, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.
Leclerc98: Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA (1998). "Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria." Proc Natl Acad Sci U S A 95(6);3059-64. PMID: 9501215
Olteanu01: Olteanu H, Banerjee R (2001). "Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation." J Biol Chem 276(38);35558-63. PMID: 11466310
Olteanu02: Olteanu H, Munson T, Banerjee R (2002). "Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase." Biochemistry 41(45);13378-85. PMID: 12416982
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