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==References==
==References==
{{reflist|1}}
{{reflist|1}}
* {{cite journal | author = Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P | date = Pt 1 | title = Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli | journal = Biochem. J. | volume = 307 | pages = 77–85 | pmid = 7717997 }}
* {{cite journal | author = Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P | date = Pt 1 | title = Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli | journal = Biochem. J. | volume = 307 | pages = 77–85 | pmid = 7717997 | pmc = 1136747 }}
* {{cite journal | author = Zhang Z, Barlow JN, Baldwin JE, Schofield CJ | date = 1997 | title = Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase | journal = Biochemistry. | volume = 36 | pages = 15999–6007 | pmid = 9398335 | doi = 10.1021/bi971823c }}
* {{cite journal | author = Zhang Z, Barlow JN, Baldwin JE, Schofield CJ | date = 1997 | title = Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase | journal = Biochemistry. | volume = 36 | pages = 15999–6007 | pmid = 9398335 | doi = 10.1021/bi971823c | issue = 50 }}
* {{cite journal | author = Pirrung MC | date = 1999 | title = Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid | journal = Acc. Chem. Res. | volume = 32 | pages = 711–718 | doi = 10.1021/ar960003 }}
* {{cite journal | author = Pirrung MC | date = 1999 | title = Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid | journal = Acc. Chem. Res. | volume = 32 | pages = 711–718 | doi = 10.1021/ar960003 }}
* {{cite journal | author = Charng YY, Chou SJ, Jiaang WT, Chen ST, Yang SF | date = 2001 | title = The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase | journal = Arch. Biochem. Biophys. | volume = 385 | pages = 179–85 | pmid = 11361015 | doi = 10.1006/abbi.2000.2138 }}
* {{cite journal | author = Charng YY, Chou SJ, Jiaang WT, Chen ST, Yang SF | date = 2001 | title = The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase | journal = Arch. Biochem. Biophys. | volume = 385 | pages = 179–85 | pmid = 11361015 | doi = 10.1006/abbi.2000.2138 | issue = 1 }}
* {{cite journal | author = Thrower JS, Blalock R 3rd Klinman JP | date = 2001 | title = Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase | journal = Biochemistry. | volume = 40 | pages = 9717–24 | pmid = 11583172 | doi = 10.1021/bi010329c }}
* {{cite journal | author = Thrower JS, Blalock R 3rd Klinman JP | date = 2001 | title = Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase | journal = Biochemistry. | volume = 40 | pages = 9717–24 | pmid = 11583172 | doi = 10.1021/bi010329c | issue = 32 }}


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Revision as of 20:24, 6 July 2010

Aminocyclopropanecarboxylate oxidase
Identifiers
EC no.1.14.17.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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: 77–85. PMC 1136747. PMID 7717997. {{cite journal}}: Check date values in: |date= (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.{{cite journal}}: 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.{{cite journal}}: 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)