In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical reaction
| aldehyde dehydrogenase (pyrroloquinoline-quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.99.3 | ||||||||
| CAS no. | 75536-77-5 | ||||||||
| 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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- an aldehyde + acceptor + H2O 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.
References
edit- Ameyama M; Adachi O (1982). "Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound". Carbohydrate Metabolism - Part D. Methods Enzymol. Vol. 89. pp. 491–497. doi:10.1016/S0076-6879(82)89084-8. ISBN 978-0-12-181989-7.
- Ameyama M, Osada K, Shinagawa E, Matsushita K, Adachi O (1981). "Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti". Agric. Biol. Chem. 45 (8): 1889–1890. doi:10.1271/bbb1961.45.1889.
- 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 (2): 654–62. doi:10.1016/0003-9861(80)90223-4. PMID 6779711.
