(R)-aminopropanol dehydrogenase

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(R)-aminopropanol dehydrogenase
Identifiers
EC no. 1.1.1.75
CAS no. 37250-13-8
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 / QuickGO
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PMC articles
PubMed articles
NCBI proteins

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

+ NAD+
 
 
 
H+
(R)-aminopropanol dehydrogenase
 
H+
 
+ NADH
 

The two substrates of this enzyme are (2R)-1-aminopropan-2-ol and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are aminoacetone, reduced NADH, and a proton. [1] [2] [3] [4]

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

  1. Enzyme 1.1.1.75 at KEGG Pathway Database.
  2. 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. hdl: 2027.42/33173 . PMID   4385233.
  3. 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. doi:10.1042/bj0990427. PMC   1265012 . PMID   5329339.
  4. 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. doi:10.1042/bj1040112. PMC   1270551 . PMID   5340733.