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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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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
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MetaCyc Reaction: 1.16.1.8

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: 1.16.1.8

Enzymes and Genes:
methionine synthase reductase : MTRR ( Homo sapiens )

Supersedes EC number: 2.1.1.135

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: 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)

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 2.1.1.13, methionine synthase. Electrons are transferred from NADPH to FAD to FMN. Defects in this enzyme lead to hereditary hyperhomocysteinemia.

Citations: [Leclerc98, Olteanu01, Olteanu02]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.16.1.8 , ENZYME:EC:1.16.1.8 , IUBMB-ExplorEnz:EC:1.16.1.8

Credits:
Revised 12-Dec-2011 by Caspi R , SRI International


References

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


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 Mon Dec 22, 2014, biocyc14.