Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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 Thu Nov 20, 2014, BIOCYC14B.