EC Tree |
2. Transferases |
2.7 Transferring phosphorus-containing groups |
2.7.1 Phosphotransferases with an alcohol group as acceptor |
ID: | 2.7.1.86 |
---|---|
Description: | NADH kinase. |
Cath: | 3.40.50.12540; 2.60.200.30; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.7.1.86 |
BRENDA Enzyme Link: | BRENDA 2.7.1.86 |
KEGG Enzyme Link: | KEGG2.7.1.86 |
BioCyc Enzyme Link: | BioCyc 2.7.1.86 |
ExPASy Enzyme Link: | ExPASy2.7.1.86 |
EC2PDB Enzyme Link: | EC2PDB 2.7.1.86 |
ExplorEnz Enzyme Link: | ExplorEnz 2.7.1.86 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.7.1.86 |
IntEnz Enzyme Link: | IntEnz 2.7.1.86 |
MEDLINE Enzyme Link: | MEDLINE 2.7.1.86 |
RHEA:12260 | ATP + NADH = ADP + H(+) + NADPH |
RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](=[*:3])(-[*:5])-[*:6].[*:8]-[OH;+0:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions. | Bieganowski P, Seidle HF, Wojcik M, Brenner C | 2006 Aug 11 | 16760478 |
Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae. | Shi F, Kawai S, Mori S, Kono E, Murata K | 2005 Jul | 15978040 |
Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana (thale cress). | Turner WL, Waller JC, Snedden WA | 2005 Jan 1 | 15347288 |