4,5:9,10-diseko-3-hidroksi-5,9,17-trioksoandrosta-1(10),2-dien-4-oatna hidrolaza
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| 4,5:9,10-diseko-3-hidroksi-5,9,17-trioksoandrosta-1(10),2-dien-4-oatna hidrolaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 3.7.1.17 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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4,5:9,10-diseko-3-hidroksi-5,9,17-trioksoandrosta-1(10),2-dien-4-oatna hidrolaza (EC 3.7.1.17, tesD (gen), hsaD (gen)) je enzim sa sistematskim imenom 4,5:9,10-diseko-3-hidroksi-5,9,17-trioksoandrosta-1(10),2-dien-4-oat hidrolaza (formira (2Z,4Z)-2-hidroksiheksa-2,4-dienoat).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1E,2Z)-3-hidroksi-5,9,17-triokso-4,5:9,10-disekoandrosta-1(10),2-dien-4-oat + H2O 3-[(3aS,4S,7aS)-7a-metil-1,5-diokso-oktahidro-1H-inden-4-il]propanoat + (2Z,4Z)-2-hidroksiheksa-2,4-dienoat
Ovaj enzim učestvuje u bakterijskoj degradaciji steroidnog prstena.
Reference[uredi | uredi kod]
- ↑ Horinouchi, M., Hayashi, T., Koshino, H., Kurita, T. and Kudo, T. (2005). „Identification of 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid, 4-hydroxy-2-oxohexanoic acid, and 2-hydroxyhexa-2,4-dienoic acid and related enzymes involved in testosterone degradation in Comamonas testosteroni TA441”. Appl. Environ. Microbiol. 71: 5275-5281. PMID 16151114.
- ↑ Van der Geize, R., Yam, K., Heuser, T., Wilbrink, M.H., Hara, H., Anderton, M.C., Sim, E., Dijkhuizen, L., Davies, J.E., Mohn, W.W. and Eltis, L.D. (2007). „A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into Mycobacterium tuberculosis survival in macrophages”. Proc. Natl. Acad. Sci. USA 104: 1947-1952. PMID 17264217.
- ↑ Lack, N., Lowe, E.D., Liu, J., Eltis, L.D., Noble, M.E., Sim, E. and Westwood, I.M. (2008). „Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis”. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64: 2-7. PMID 18097091.
- ↑ Lack, N.A., Yam, K.C., Lowe, E.D., Horsman, G.P., Owen, R.L., Sim, E. and Eltis, L.D. (2010). „Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism”. J. Biol. Chem. 285: 434-443. PMID 19875455.
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.