EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 4.2.1.93

Names

Accepted name:
ATP-dependent NAD(P)H-hydrate dehydratase
Other names:
ATP-dependent H4NAD(P)OH dehydratase
reduced nicotinamide adenine dinucleotide hydrate dehydratase
(6S)-β-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing)
(6S)-6-β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
Systematic name:
(6S)-6β-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)

Reactions

Comments:

Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio [4]. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H [3,4]. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase) [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047453
UniProtKB/Swiss-Prot: (42) [show] [UniProt]

References

  1. Meinhart, J.O., Chaykin, S. and Krebs, E.G.
    Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative to reduced diphosphopyridine nucleotide.
    J. Biol. Chem. 220: 821-829 (1956). [PMID: 13331940]
  2. Regueiro Varela, B., Amelunxen, R. and Grisolia, S.
    Synthesis and degradation of monohydroxytetrahydronicotinamide adenine dinucleotide phosphate.
    Physiol. Chem. Phys. 2: 445-454 (1970).
  3. Acheson, S. A., Kirkman, H. N., Wolfenden, R.
    Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration.
    Biochemistry 27: 7371-7375 (1988). [PMID: 3061454]
  4. Marbaix, A. Y., Noel, G., Detroux, A. M., Vertommen, D., Van Schaftingen, E., Linster, C. L.
    Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.
    J. Biol. Chem. 286: 41246-41252 (2011). [PMID: 21994945]

[EC 4.2.1.93 created 1992, modified 2012]