1,8-Cineol 2-endo-monooksigenaza

1,8-Cineol 2-endo-monooksigenaza
Identifikatori
EC broj	1.14.13.156
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

1,8-Cineol 2-endo-monooksigenaza (EC 1.14.13.156, P450cin, CYP176A, CYP176A1) je enzim sa sistematskim imenom 1,8-cineol,NADPH:kiseonik oksidoreduktaza (2-endo-hidroksilacija).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

1,8-cineol + NADPH + H⁺ + O₂

\rightleftharpoons

2-endo-hidroksi-1,8-cineol + NADP⁺ + H₂O

Ovaj enzim je hem-tiolatni protein (P-450) koji koristi flavodoksinu sličnog redoks partnera da redukuje gvožđehema.

Reference uredi

↑ Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. (2002). „Cytochrome P450_cin (CYP176A), isolation, expression, and characterization”. J. Biol. Chem. 277: 27725-27732. PMID 12016226.
↑ Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. (2004). „Crystal structure of P450_cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450_cam”. Biochemistry 43: 9487-9494. PMID 15260491.
↑ Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. (2007). „Electron transfer between cytochrome P450_cin and its FMN-containing redox partner, cindoxin”. J. Biol. Chem. 282: 27006-27011. PMID 17606612.
↑ Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. (2008). „The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin”. J. Biol. Chem. 283: 10804-10812. PMID 18270198.

Literatura uredi

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.

Spoljašnje veze uredi

MeSH 1,8-cineole+2-endo-monooxygenase

[1] Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. (2002). „Cytochrome P450_cin (CYP176A), isolation, expression, and characterization”. J. Biol. Chem. 277: 27725-27732. PMID 12016226.

[2] Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. (2004). „Crystal structure of P450_cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450_cam”. Biochemistry 43: 9487-9494. PMID 15260491.

[3] Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. (2007). „Electron transfer between cytochrome P450_cin and its FMN-containing redox partner, cindoxin”. J. Biol. Chem. 282: 27006-27011. PMID 17606612.

[4] Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. (2008). „The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin”. J. Biol. Chem. 283: 10804-10812. PMID 18270198.

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