Aminocyclopropanecarboxylate oxidase

From Wikipedia, the free encyclopedia

In enzymology, an aminocyclopropanecarboxylate oxidase (EC 1.14.17.4) is an enzyme that catalyzes the chemical reaction

1-aminocyclopropane-1-carboxylate + ascorbate + O₂ $\rightleftharpoons$ ethylene + cyanide + dehydroascorbate + CO₂ + 2 H₂O

The 3 substrates of this enzyme are 1-aminocyclopropane-1-carboxylate, ascorbate, and O₂, whereas its 5 products are ethylene, cyanide, dehydroascorbate, CO₂, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming). Other names in common use include ACC oxidase, and ethylene-forming enzyme.

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1W9Y and 1WA6.

[edit] References

IUBMB entry for 1.14.17.4
BRENDA references for 1.14.17.4 (Recommended.)
PubMed references for 1.14.17.4
PubMed Central references for 1.14.17.4
Google Scholar references for 1.14.17.4
Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P (Pt 1). "Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli". Biochem. J. 307: 77–85. PMID 7717997.
Zhang Z, Barlow JN, Baldwin JE, Schofield CJ (1997). "Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase". Biochemistry. 36: 15999–6007. doi:10.1021/bi971823c. PMID 9398335.
Pirrung MC (1999). "Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid". Acc. Chem. Res. 32: 711–718. doi:10.1021/ar960003+.
Charng YY, Chou SJ, Jiaang WT, Chen ST, Yang SF (2001). "The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase". Arch. Biochem. Biophys. 385: 179–85. doi:10.1006/abbi.2000.2138. PMID 11361015.
Thrower JS, Blalock R 3rd Klinman JP (2001). "Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase". Biochemistry. 40: 9717–24. doi:10.1021/bi010329c. PMID 11583172.