1-aminocyclopropane-1-carboxylate deaminase

In enzymology, a 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7) is an enzyme that catalyzes the chemical reaction

1-aminocyclopropane-1-carboxylate + H₂O 2-oxobutanoate + NH₃

Thus, the two substrates of this enzyme are 1-aminocyclopropane-1-carboxylate and H₂O, whereas its two products are 2-oxobutanoate and NH₃.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also called 1-aminocyclopropane-1-carboxylate endolyase (deaminating). This enzyme participates in propanoate metabolism. It employs one cofactor, pyridoxal phosphate.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1RQX, 1TYZ, 1TZ2, 1TZJ, 1TZK, and 1TZM.

References

IUBMB entry for 3.5.99.7
BRENDA references for 3.5.99.7 (Recommended.)
PubMed references for 3.5.99.7
PubMed Central references for 3.5.99.7
Google Scholar references for 3.5.99.7
Honma M and Shimomura T (1978). "Metabolism of 1-aminocyclopropane-1-carboxylic acid". Agric. Biol. Chem. 42: 1825–1831.
Wakatsuki S, Yokoi D, Murakami T, Honma M and Tanaka I (2000). "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus". J. Biol. Chem. 275: 34557–34565. doi:10.1074/jbc.M004681200.