| EC |
1.6.1.1 |
| Accepted name: |
NAD(P)+ transhydrogenase (Si-specific) |
| Reaction: |
NADPH + NAD+ = NADP+ + NADH |
| Other name(s): |
pyridine nucleotide transhydrogenase; transhydrogenase; NAD(P)+ transhydrogenase; nicotinamide adenine dinucleotide (phosphate) transhydrogenase; NAD+ transhydrogenase; NADH transhydrogenase; nicotinamide nucleotide transhydrogenase; NADPH-NAD+ transhydrogenase; pyridine nucleotide transferase; NADPH-NAD+ oxidoreductase; NADH-NADP+-transhydrogenase; NADPH:NAD+ transhydrogenase; H+-Thase; non-energy-linked transhydrogenase; NADPH:NAD+ oxidoreductase (B-specific); NAD(P)+ transhydrogenase (B-specific) |
| Systematic name: |
NADPH:NAD+ oxidoreductase (Si-specific) |
| Comments: |
The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). It is Si-specific with respect to both NAD+ and NADP+. See EC 1.6.1.3, NAD(P)+ transhydrogenase, for enzymes whose stereo specificity is not known. |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-18-0 |
| References: |
| 1. |
Humphrey, G.F. The distribution and properties of transhydrogenase from animal tissues. Biochem. J. 65 (1957) 546–550. [PMID: 13412660] |
| 2. |
You, K.-S. Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions. CRC Crit. Rev. Biochem. 17 (1985) 313–451. [PMID: 3157549] |
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| [EC 1.6.1.1 created 1961, modified 1986, modified 2013] |
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