Katehol 2,3-dioksigenaza
Prijeđi na navigaciju
Prijeđi na pretragu
Katehol 2,3-dioksigenaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 1.13.11.2 | ||||||||
CAS broj | 9029-46-3 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
Katehol 2,3-dioksigenaza (EC 1.13.11.2, 2,3-pirokatehaza, katehol 2,3-oksigenaza, katehol oksigenaza, metapirokatehaza, pirokatehol 2,3-dioksigenaza) je enzim sa sistematskim imenom katehol:kiseonik 2,3-oksidoreduktaza (deciklizacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- katehol + O2 2-hidroksimukonat semialdehid
Za rad ovog enzima neohodan je Fe(II). Enzim iz Alcaligenes sp. vrste O-1 takođe može da katalizuje reakciju:
- 2,3-dihidroksibenzensulfonat + O2</sib> + H2O 2-hidroksimukonat + bisulfit
On se naziva 2,3-dihidroksibenzensulfonat 2,3-dioksigenaza.
Reference[uredi | uredi kod]
- ↑ Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. (1994). „Dioxygenation and spontaneous deamination of 2-aminobenzene sulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid”. Biochem. J. 300: 429-436. PMID 8002948.
- ↑ Junker, F., Leisinger, T. and Cook, A.M. (1994). „3-Sulphocatechol dioxygenase and other dioxygenases (1.13.11.2 and 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1”. J. Gen. Microbiol. 140: 1713-1722. PMID 8075807.
- ↑ Hayaishi, O. (1963). „Direct oxygenation by O2, oxygenases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 8 (2nd izd.). New York: Academic Press. str. 353-371.
- ↑ Kojima, Y., Itada, N. and Hayaishi, O. (1961). „Metapyrocatechase: a new catechol-cleaving enzyme”. J. Biol. Chem. 236: 2223-2228. PMID 13757654.
- ↑ Nozaki, M., Kagamiyama, H. and Hayaishi, O. (1963). „Metapyrocatechase. I. Purification, crystallization and some properties”. Biochem. Z. 338: 582-590. PMID 14087325.
Literatura[uredi | uredi kod]
- 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.
- Hayaishi, O. (1963). „Direct oxygenation by O2, oxygenases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 8 (2nd izd.). New York: Academic Press. str. 353-371.