| Entry |
|
| Name |
[methionine synthase] reductase;
methionine synthase cob(II)alamin reductase (methylating);
methionine synthase reductase;
[methionine synthase]-cobalamin methyltransferase (cob(II)alamin reducing)
|
| Class |
Oxidoreductases;
Oxidizing metal ions;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
[methionine synthase]-methylcob(I)alamin,S-adenosylhomocysteine:NADP+ oxidoreductase
|
| Reaction(IUBMB) |
2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + H+ + 2 S-adenosyl-L-methionine [RN: R05182]
|
| Reaction(KEGG) |
|
| Substrate |
[methionine synthase]-methylcob(I)alamin [CPD: C06410];
S-adenosylhomocysteine [CPD: C00021];
NADP+ [CPD: C00006]
|
| Product |
[methionine synthase]-cob(II)alamin [CPD: C06409];
NADPH [CPD: C00005];
H+ [CPD: C00080];
S-adenosyl-L-methionine [CPD: C00019]
|
| Comment |
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.
|
| Orthology |
| [methionine synthase] reductase |
|
| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | SHR: | | OAA: | | GGA: | | MGP: | | TGU: | | ACS: | | XTR: | | DRE: | | TRU: | | OLA: | | BFO: | | CIN: | | SPU: | | DME: | | DAN: | | DER: | | DWI: | | DGR: | | AGA: | | AAG: | | TCA: | | PHU: | | ISC: | | CEL: | | CBR: | | BMY: | | TSP: | | SMM: | | NVE: | | HMG: | | TAD: | | AQU: | | MBR: | | NGR: | | DPP: | | PIF: | | » show all
 |
| Reference |
|
| Authors |
Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA. |
| Title |
Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3059-64. |
| Organism |
|
| Reference |
|
| Authors |
Olteanu H, Banerjee R. |
| Title |
Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. |
| Journal |
J. Biol. Chem. 276 (2001) 35558-63. |
| Organism |
|
| Reference |
|
| Authors |
Olteanu H, Munson T, Banerjee R. |
| Title |
Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase. |
| Journal |
Biochemistry. 41 (2002) 13378-85. |
| Organism |
|
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 207004-87-3 |