NAD(P)+ transhydrogenase (Re/Si-specific)
| NAD(P)+ transhydrogenase (Re/Si-specific | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.6.1.2 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
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. 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). This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes 1NM5, 1PNO, 1PNQ, 1PT9, 1PTJ, 1U28, 1U2D, 1U2G, 1U31, 1X13, 1X14, 1X15, 1XLT, 2BRU, 2FR8, 2FRD, 2FSV, 2OO5, and 2OOR.
References
- Everse, J., Anderson, B. and You, K. (Eds.), The Pyridine Nucleotide Coenzymes, The Pyridine Nucleotide Coenzymes, New York, 1982, p. 279-324.
- You KS; Oppenheimer, Norman J. (1985). "Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions". CRC. Crit. Rev. Biochem. 17 (4): 313–451. doi:10.3109/10409238509113625. PMID 3157549.
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