NAD(P)+ transhydrogenase (Re/Si-specific)

NAD(P) transhydrogenase
NAD(P) transhydrogenase heterotrimer, Rhodospirillum rubrum
Identifiers
Symbol?
PfamPF02233
TCDB3.D.2
OPM superfamily410
OPM protein4o9u
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NAD(P)+ transhydrogenase (Re/Si-specific
Identifiers
EC no.1.6.1.2
CAS no.9014-18-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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. 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.


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