NAD(P)+ transhydrogenase (Re/Si-specific)
In enzymology, a NAD(P)+ transhydrogenase (Re/Si-specific (EC 1.6.1.2) is an enzyme that catalyzes the chemical reaction
- NADPH + NAD+ NADP+ + NADH
| NAD(P) transhydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ? | ||||||||
| Pfam | PF02233 | ||||||||
| TCDB | 3.D.2 | ||||||||
| OPM superfamily | 410 | ||||||||
| OPM protein | 4o9u | ||||||||
| |||||||||
| NAD(P)+ transhydrogenase (Re/Si-specific | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.6.1.2 | ||||||||
| CAS number | 9014-18-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are NADPH and NAD+, whereas its two products are NADP+ and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. This enzyme participates in nicotinate and nicotinamide metabolism.
Nomenclature
The systematic name of this enzyme class is NADPH:NAD+ oxidoreductase (Re/Si-specific). Other names in common use include 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, energy-linked transhydrogenase, and NAD(P)+ transhydrogenase (AB-specific).
References
Further reading
- Fisher RR, Earle SR (1982). "Membrane-Bournd Pyridine Dinucleotide Transhydrogenases". In Everse J, Anderson B, You K (eds.). The Pyridine Nucleotide Coenzymes. Burlington: Elsevier Science. pp. 279–324. ISBN 978-0-323-15084-2.
- You KS (1985). "Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions". CRC Critical Reviews in Biochemistry. 17 (4): 313–451. doi:10.3109/10409238509113625. PMID 3157549.