(R)-aminopropanol dehydrogenase

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(R)-aminopropanol dehydrogenase
Identifiers
EC number1.1.1.75
CAS number37250-13-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a (R)-aminopropanol dehydrogenase (EC 1.1.1.75) is an enzyme that catalyzes the chemical reaction

(R)-1-aminopropan-2-ol + NAD+ aminoacetone + NADH + H+

Thus, the two substrates of this enzyme are (R)-1-aminopropan-2-ol and NAD+, whereas its 3 products are aminoacetone, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-1-aminopropan-2-ol:NAD+ oxidoreductase. Other names in common use include L-aminopropanol dehydrogenase, 1-aminopropan-2-ol-NAD+ dehydrogenase, L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase, 1-aminopropan-2-ol-dehydrogenase, DL-1-aminopropan-2-ol: NAD+ dehydrogenase, and L(+)-1-aminopropan-2-ol-NAD+/NADP+ oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It requires potassium as a cofactor.

References[edit]

  • Dekker EE, Swain RR (1968). "Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli" (PDF). Biochim. Biophys. Acta. 158 (2): 306–7. doi:10.1016/0304-4165(68)90150-5. PMID 4385233.
  • Tuner JM (1966). "Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in Escherichia coli". Biochem. J. 99 (2): 427–33. PMC 1265012. PMID 5329339.
  • Turner JM (1967). "Microbial metabolism of amino ketones: l-1-Aminopropan-2-ol dehydrogenase and l-threonine dehydrogenase in Escherichia coli". Biochem. J. 104 (1): 112–21. PMC 1270551. PMID 5340733.