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B-karoten 15,15'-monooksigenaza
Identifikatori
EC broj	1.14.99.36
CAS broj	37256-60-3
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

B-karoten 15,15'-monooksigenaza (EC 1.14.99.36, beta-karotenska 15,15'-dioksigenaza, karotenska dioksigenaza, karotenska 15,15'-dioksigenaza, BCMO1 (gen)) je enzim sa sistematskim imenom beta-karoten:kiseonik 15,15'-oksidoreduktaza (15,15'-epoksidacija, razgradnja veze).^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju

beta-karoten + O₂

\rightleftharpoons

2 sve-trans retinal (sveukupna reakcija)

(1a) beta-karoten + O₂ + AH₂

\rightleftharpoons

beta-karoten 15,15' epoksid + H₂O + A

(1b) beta-karoten 15,15' epoksid + H₂O

\rightleftharpoons

15,15'-dihidroksi-beta-karoten

(1c) 15,15'-dihidroksi-beta-karoten + A

\rightleftharpoons

2 sve-trans retinal + AH₂

Za rad ovog enzim su neophodne žučne soli i Fe(II).

Reference

↑ Goodman, D.S., Huang, H.S. and Shiratori, T. (1966). „Mechanism of the biosynthesis of vitamin A from β-carotene”. J. Biol. Chem. 241: 1929-1932. PMID 5946623.
↑ Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. (1967). „The enzymatic conversion of all-trans β-carotene into retinal”. J. Biol. Chem. 242: 3543-3554.
↑ Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. (2001). „The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal”. Angew. Chem. 40: 2614-2616.
↑ Kim, Y.S. and Oh, D.K. (2009). „Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal”. Biotechnol. Lett. 31: 403-408. PMID 18979213.

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 Beta-carotene+15,15'-monooxygenase

[1] Goodman, D.S., Huang, H.S. and Shiratori, T. (1966). „Mechanism of the biosynthesis of vitamin A from β-carotene”. J. Biol. Chem. 241: 1929-1932. PMID 5946623.

[2] Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. (1967). „The enzymatic conversion of all-trans β-carotene into retinal”. J. Biol. Chem. 242: 3543-3554.

[3] Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. (2001). „The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal”. Angew. Chem. 40: 2614-2616.

[4] Kim, Y.S. and Oh, D.K. (2009). „Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal”. Biotechnol. Lett. 31: 403-408. PMID 18979213.

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