PROFILPELAJAR.COM

Aminociklopropankarboksilat oksidaza
Identifikatori
EC broj	1.14.17.4
CAS broj	98668-53-2
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

Aminociklopropankarboksilat oksidaza (EC 1.14.17.4, ACC oksidaza, etilen-formirajući enzim) je enzim sa sistematskim imenom 1-aminociklopropan-1-karboksilat oksigenaza (formira etilen).^[1]^[2]^[3]^[4]^[5] Ovaj enzim katalizuje sledeću hemijsku reakciju

1-aminociklopropan-1-karboksilat + askorbat + O₂

\rightleftharpoons

etilen + cijanid + dehidroaskorbat + CO₂ + 2H₂O

Ovaj enzim sadrži gvožđe nevezano za hem. Za njegov rad je neophodan CO₂.

Reference

↑ Zhang, Z.H., Schofield, C.J., Baldwin, J.E., Thomas, P. and John, P. (1995). „Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli”. Biochem. J. 307: 77-85. PMID 7717997.
↑ Zhang, Z.H., Barlow, J.N., Baldwin, J.E. and Schofield, C.J. (1997). „Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase”. Biochemistry 36: 15999-16007. PMID 9398335.
↑ Pirrung, M.C. (1999). „Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid”. Acc. Chem. Res. 32: 711-718.
↑ Charng, Y., Chou, S.J., Jiaang, W.T., Chen, S.T. and Yang, S.F. (2001). „The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase”. Arch. Biochem. Biophys. 385: 179-185. PMID 11361015.
↑ Thrower, J.S., Blalock, R. and Klinman, J.P. (2001). „Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase”. Biochemistry 40: 9717-9724. PMID 11583172.

Literatura

Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.

Vanjske veze

MeSH Aminocyclopropanecarboxylate+oxidase

[1] Zhang, Z.H., Schofield, C.J., Baldwin, J.E., Thomas, P. and John, P. (1995). „Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli”. Biochem. J. 307: 77-85. PMID 7717997.

[2] Zhang, Z.H., Barlow, J.N., Baldwin, J.E. and Schofield, C.J. (1997). „Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase”. Biochemistry 36: 15999-16007. PMID 9398335.

[3] Pirrung, M.C. (1999). „Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid”. Acc. Chem. Res. 32: 711-718.

[4] Charng, Y., Chou, S.J., Jiaang, W.T., Chen, S.T. and Yang, S.F. (2001). „The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase”. Arch. Biochem. Biophys. 385: 179-185. PMID 11361015.

[5] Thrower, J.S., Blalock, R. and Klinman, J.P. (2001). „Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase”. Biochemistry 40: 9717-9724. PMID 11583172.

[1]

[2]

[3]

[4]

[5]