KEGG   ENZYME: 1.1.1.75
Entry
EC 1.1.1.75                 Enzyme                                 
Name
(R)-aminopropanol dehydrogenase;
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;
L(+)-1-aminopropan-2-ol-NAD+/NADP+ oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(R)-1-aminopropan-2-ol:NAD+ oxidoreductase
Reaction(IUBMB)
(R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+ [RN:R03759]
Reaction(KEGG)
R03759
Substrate
(R)-1-aminopropan-2-ol [CPD:C03194];
NAD+ [CPD:C00003]
Product
aminoacetone [CPD:C01888];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
Requires K+.
History
EC 1.1.1.75 created 1972
Pathway
ec00260  Glycine, serine and threonine metabolism
ec01100  Metabolic pathways
Reference
1  [PMID:4385233]
  Authors
Dekker EE, Swain RR.
  Title
Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli.
  Journal
Biochim Biophys Acta 158:306-7 (1968)
DOI:10.1016/0304-4165(68)90150-5
Reference
2  [PMID:5329339]
  Authors
Tuner JM.
  Title
Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escerichia coli.
  Journal
Biochem J 99:427-33 (1966)
DOI:10.1042/bj0990427
Reference
3  [PMID:5340733]
  Authors
Turner JM.
  Title
Microbial metabolism of amino ketones. L-1-aminopropan-2-ol dehydrogenase and L-threonine dehydrogenase in Escherichia coli.
  Journal
Biochem J 104:112-21 (1967)
DOI:10.1042/bj1040112
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.75
IUBMB Enzyme Nomenclature: 1.1.1.75
ExPASy - ENZYME nomenclature database: 1.1.1.75
BRENDA, the Enzyme Database: 1.1.1.75
CAS: 37250-13-8
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