ATP-dependent NAD(P)H-hydrate dehydratase
| ATP-dependent NAD(P)H-hydrate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.93 | ||||||||
| 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, an ATP-dependent NAD(P)H-hydrate dehydratase (EC 4.2.1.93) is an enzyme that catalyzes the chemical reaction
- ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide ADP + phosphate + NADH
The 3 substrates of this enzyme are ATP, (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine, and dinucleotide, whereas its 3 products are ADP, phosphate, and NADH.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleot ide hydro-lyase (ATP-hydrolysing; NADH-forming). Other names in common use include reduced nicotinamide adenine dinucleotide hydrate dehydratase, ATP-dependent H4NAD(P)+OH dehydratase, (6S)-beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-, and dinucleotide hydro-lyase(ATP-hydrolysing).
References
- Acheson SA, Kirkman HN, Wolfenden R (1988). "Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration". Biochemistry. 27 (19): 7371–5. doi:10.1021/bi00419a030. PMID 3061454.
- MEINHART JO, CHAYKIN S, KREBS EG (1956). "Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative to reduced diphosphopyridine nucleotide". J. Biol. Chem. 220 (2): 821–9. PMID 13331940.
- Regueiro V, Campos MA, Pons J, Alberti S, Bengoechea JA (2006). "The uptake of a Klebsiella pneumoniae capsule polysaccharide mutant triggers an inflammatory response by human airway epithelial cells". Microbiology. 152 (Pt 2): 555–66. doi:10.1099/mic.0.28285-0. PMID 16436443.