Bleomicinska hidrolaza
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| Bleomicinska hidrolaza | |||||||||
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| Bleomicinska hidrolaza hexamer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.22.40 | ||||||||
| CAS broj | 53096-17-6 | ||||||||
| 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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Bleomicinska hidrolaza (EC 3.4.22.40, aminopeptidaza C (laktococcus lactis)) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Inaktivacija bleomicina B2 (citotoksičnog glikometalopeptida) putem hidrolize karboksiamidne veze beta-aminoalanina. Takođe ispoljava opštu aminopeptidaznu aktivnost. Specifičnost varira u zavistnosti od izvora enzima, ali su aminokiselinski arilamidi aminokiselina Met, Leu i Ala preferentni
Ovaj enzim je homoheksamer, pri čemu monomeri imaju papainu-sličnu tercijarnu strukturu.
Reference[uredi - уреди | uredi kôd]
- ↑ Brömme, D., Rossi, A.B., Smeekens, S.P., Anderson, D.C. & Payan, D.G. (1996). „Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization”. Biochemistry 35: 6706-6714. PMID 8639621.
- ↑ Adachi, H., Tsujimoto, M., Fukasawa, M., Sato, Y., Arai, H., Inoue, K. and Nishimura, T. (1997). „cDNA cloning and expression of chicken aminopeptidase H, possessing endopeptidase as well as aminopeptidase activity”. Eur. J. Biochem. 245: 283-288. PMID 9151954.
- ↑ Zheng, W., Johnston, S.A. & Joshua-Tor, L. (1998). „The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase”. Cell 93: 103-109. PMID 9546396.
- ↑ Mistou, M.Y. & Gripon, J.C. (1998). „Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase”. Biochim. Biophys. Acta 1383: 63-70. PMID 9546047.
Literatura[uredi - уреди | uredi kôd]
- 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. http://books.google.com/books/about/Fundamentals_of_enzymology.html?id=8uvwAAAAMAAJ.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. http://books.google.com/books/about/Advances_in_Enzymology_and_Related_Areas.html?id=Pmh8yToeuloC.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. http://www.garlandscience.com/textbooks/0815323042.asp?type=reviews.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. http://books.google.com/books/about/Enzyme_Kinetics.html?id=T60oAAAAYAAJ.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. http://books.google.com/books/about/Evaluation_of_Enzyme_Inhibitors_in_Drug.html?id=l2rMy8QNUk0C.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. http://books.google.com/books/about/Biochemical_pathways.html?id=081qAAAAMAAJ.
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