Aldehyde dehydrogenase (pyrroloquinoline-quinone)

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In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical reaction

an aldehyde + acceptor + H₂O $\rightleftharpoons$ a carboxylate + reduced acceptor

The 3 substrates of this enzyme are aldehyde, acceptor, and H₂O, whereas its two products are carboxylate and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with other acceptors. The systematic name of this enzyme class is aldehyde:(pyrroloquinoline-quinone) oxidoreductase. This enzyme is also called aldehyde dehydrogenase (acceptor). This enzyme participates in 4 metabolic pathways: fatty acid metabolism, pyruvate metabolism, propanoate metabolism, and butanoate metabolism. It employs one cofactor, PQQ.

[edit] References

IUBMB entry for 1.2.99.3
BRENDA references for 1.2.99.3 (Recommended.)
PubMed references for 1.2.99.3
PubMed Central references for 1.2.99.3
Google Scholar references for 1.2.99.3
Ameyama M and Adachi O (1982). "Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound". Methods Enzymol. 89: 491–497.
Ameyama M, Osada K, Shinagawa E, Matsushita K and Adachi O (1981). "Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti". Agric. Biol. Chem. 45: 1189–1890.
Patel RN, Hou CT, Derelanko P, Felix A (1980). "Purification and properties of a heme-containing aldehyde dehydrogenase from Methylosinus trichosporium". Arch. Biochem. Biophys. 203: 654–62. doi:10.1016/0003-9861(80)90223-4. PMID 6779711.