NAD(P)+ transhydrogenase (B-specific)
NAD(P)+ transhydrogenase (B-specific) | |||||||||
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Identifiers | |||||||||
EC number | 1.6.1.1 | ||||||||
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 / EGO | ||||||||
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In enzymology, a NAD(P)+ transhydrogenase (B-specific) (EC 1.6.1.1) is an enzyme that catalyzes the chemical reaction
- NADP+ + NADH+ NADPH+ + NAD+
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 (B-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, non-energy-linked transhydrogenase, and NAD(P)+ transhydrogenase (B-specific). This enzyme participates in nicotinate and nicotinamide metabolism. It employs one cofactor, FAD.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1D4O, 1DJL, 1E3T, 1F8G, 1HZZ, 1L7D, and 1L7E.
References
- HUMPHREY GF (1957). "The distribution and properties of transhydrogenase from animal tissues". Biochem. J. 65 (3): 546–50. PMC 1199910. PMID 13412660.
- 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.