B-karoten 15,15'-monooksigenaza
| 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 | ||||||||
| |||||||||
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 2 sve-trans retinal (sveukupna reakcija)
- (1a) beta-karoten + O2 + AH2 beta-karoten 15,15' epoksid + H2O + A
- (1b) beta-karoten 15,15' epoksid + H2O 15,15'-dihidroksi-beta-karoten
- (1c) 15,15'-dihidroksi-beta-karoten + A 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
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
