KEGG   ENZYME: 1.2.99.3Help
Entry
EC 1.2.99.3                 Enzyme                                 

Name
aldehyde dehydrogenase (pyrroloquinoline-quinone);
aldehyde dehydrogenase (acceptor)
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With other acceptors
BRITE hierarchy
Sysname
aldehyde:(pyrroloquinoline-quinone) oxidoreductase
Reaction(IUBMB)
an aldehyde + acceptor + H2O = a carboxylate + reduced acceptor [RN:R00544]
Reaction(KEGG)
Substrate
aldehyde [CPD:C00071];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Product
carboxylate [CPD:C00060];
reduced acceptor [CPD:C00030]
Comment
A quinoprotein. Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde.
History
EC 1.2.99.3 created 1983, modified 1989
Pathway
Fatty acid degradation
Pyruvate metabolism
Propanoate metabolism
Reference
1
  Authors
Ameyama, M. and Adachi, O.
  Title
Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound.
  Journal
Methods Enzymol. 89 (1982) 491-497.
Reference
2
  Authors
Ameyama, M., Osada, K., Shinagawa, E., Matsushita, K. and Adachi, O.
  Title
Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti.
  Journal
Agric. Biol. Chem. 45 (1981) 1189-1890.
Reference
3  [PMID:6779711]
  Authors
Patel RN, Hou CT, Derelanko P, Felix A.
  Title
Purification and properties of a heme-containing aldehyde dehydrogenase from Methylosinus trichosporium.
  Journal
Arch. Biochem. Biophys. 203 (1980) 654-62.
  Organism
Methylosinus trichosporium
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
75536-77-5

DBGET integrated database retrieval system