EC number:1.16.1.8
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.16 Oxidizing metal ions |
| 1.16.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.16.1.8 |
|---|---|
| Description: | [Methionine synthase] reductase. |
| Alternative Name: |
Methionine synthase reductase. Methionine synthase cob(II)alamin reductase (methylating). reducing). [Methionine synthase]-cobalamin methyltransferase (cob(II)alamin |
| Cath: | 1.10.1240.10; 1.10.288.10; 3.20.20.20; 3.20.20.330; 3.40.109.40; 3.40.50.80; 1.20.990.10; 2.40.30.10; 3.40.50.280; 3.10.196.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.16.1.8 |
| BRENDA Enzyme Link: | BRENDA 1.16.1.8 |
| KEGG Enzyme Link: | KEGG1.16.1.8 |
| BioCyc Enzyme Link: | BioCyc 1.16.1.8 |
| ExPASy Enzyme Link: | ExPASy1.16.1.8 |
| EC2PDB Enzyme Link: | EC2PDB 1.16.1.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.16.1.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.16.1.8 |
| IntEnz Enzyme Link: | IntEnz 1.16.1.8 |
| MEDLINE Enzyme Link: | MEDLINE 1.16.1.8 |
| RHEA:23908 | 2 [methionine synthase]-methylcob(III)alamin + H(+) + NADP(+) + 2 S-adenosyl-L-homocysteine = 2 [methionine synthase]-cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine |
| RULE(radius=1) | [*:1]-[Co-3;H0:2](-[*:3])(-[*:4])(-[*:5])(-[*:6])-[CH3;+0:7].[*:8]-[Co-3;H0:9](-[*:10])(-[*:11])(-[*:12])(-[*:13])-[CH3;+0:14].[*:15]-[S;H0;+0:16]-[*:17].[*:18]-[S;H0;+0:19]-[*:20].[*:21]-[c;H0;+0:22]1:[cH;+0:23]:[cH;+0:24]:[cH;+0:25]:[n+;H0:26](-[*:27]):[cH;+0:28]:1.[H+;H0:29]>>[*:21]-[C;H0;+0:22]1=[CH;+0:28]-[N;H0;+0:26](-[*:27])-[CH;+0:25]=[CH;+0:24]-[CH2;+0:23]-1.[*:1]-[Co-3;H0:2](-[*:3])(-[*:4])(-[*:5])-[*:6].[*:8]-[Co-3;H0:9](-[*:10])(-[*:11])(-[*:12])-[*:13].[*:15]-[S+;H0:16](-[*:17])-[CH3;+0:7].[*:18]-[S+;H0:19](-[*:20])-[CH3;+0:14] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. | Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA | 1998 Mar 17 | 9501215 |
| Differences in the efficiency of reductive activation of methionine synthase and exogenous electron acceptors between the common polymorphic variants of human methionine synthase reductase. | Olteanu H, Munson T, Banerjee R | 2002 Nov 12 | 12416982 |
| Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. | Olteanu H, Banerjee R | 2001 Sep 21 | 11466310 |