Aminocyclopropanecarboxylate oxidase: Difference between revisions
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[[Category:EC 1.14.17]] |
[[Category:EC 1.14.17]] |
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[[Category:Enzymes of known structure]] |
[[Category:Enzymes of known structure]] |
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[[sr:Aminociklopropankarboksilat oksidaza]] |
Revision as of 09:42, 16 April 2013
Aminocyclopropanecarboxylate oxidase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.17.4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, an aminocyclopropanecarboxylate oxidase (EC 1.14.17.4) is an enzyme that catalyzes the chemical reaction
- 1-aminocyclopropane-1-carboxylate + ascorbate + O2 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.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1W9Y and 1WA6.
References
- 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 (Pt 1): 77–85. PMC 1136747. PMID 7717997.
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(help)CS1 maint: multiple names: authors list (link) - 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 (50): 15999–6007. doi:10.1021/bi971823c. PMID 9398335.
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: CS1 maint: multiple names: authors list (link) - 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 (1): 179–85. doi:10.1006/abbi.2000.2138. PMID 11361015.
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: CS1 maint: multiple names: authors list (link) - Thrower JS, Blalock R 3rd Klinman JP (2001). "Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase". Biochemistry. 40 (32): 9717–24. doi:10.1021/bi010329c. PMID 11583172.
{{cite journal}}
: CS1 maint: numeric names: authors list (link) - Michael C. Pirrung, Lynn M. Kaiser, Jrlung Chen (1993). "1. Purification and properties of the apple fruit ethylene-forming enzyme". Biochemistry. 32 (32): 7445–50. doi:10.1021/bi00080a015. PMID 8338842.
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at position 3 (help)CS1 maint: multiple names: authors list (link)