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3-hidroksi-4-oksohinolin 2,4-dioksigenaza
Identifikatori
EC broj	1.13.11.47
CAS broj	238093-32-8
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

3-hidroksi-4-oksohinolin 2,4-dioksigenaza (EC 1.13.11.47, (1H)-3-hidroksi-4-oksohinolinska 2,4-dioksigenaza, 3-hidroksi-4-okso-1,4-dihidrohinolinska 2,4-dioksigenaza, 3-hidroksi-4(1H)-on, 2,4-dioksigenaza, hinolin-3,4-diol 2,4-dioksigenaza) je enzim sa sistematskim imenom 3-hidroksi-1H-hinolin-4-on 2,4-dioksigenaza (formira CO).^[1]^[2]^[3] Ovaj enzim katalizuje sledeću hemijsku reakciju

3-hidroksi-1H-hinolin-4-on + O₂

\rightleftharpoons

N-formilantranilat + CO

Ovaj enzim ne sadrži metalni centar ili organski kofaktor.

Reference

↑ Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. (1994). „A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline”. FEMS Microbiol. Lett. 117: 299-304.
↑ Bauer, I., Max, N., Fetzner, S. and Lingens, F. (1996). „2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1”. Eur. J. Biochem. 240: 576-583. PMID 8856057.
↑ Fischer, F., Kunne, S. and Fetzner, S. (1999). „Bacterial 2,4-dioxygenases: new members of the hydrolase-fold superfamily of enzymes functionally related to serine hydrolases”. J. Bacteriol. 181: 5725-5733. PMID 10482514.

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 3-hydroxy-4-oxoquinoline+2,4-dioxygenase

[1] Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. (1994). „A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline”. FEMS Microbiol. Lett. 117: 299-304.

[2] Bauer, I., Max, N., Fetzner, S. and Lingens, F. (1996). „2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1”. Eur. J. Biochem. 240: 576-583. PMID 8856057.

[3] Fischer, F., Kunne, S. and Fetzner, S. (1999). „Bacterial 2,4-dioxygenases: new members of the hydrolase-fold superfamily of enzymes functionally related to serine hydrolases”. J. Bacteriol. 181: 5725-5733. PMID 10482514.

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