Subtilizin
(Preusmjereno sa stranice ALK-enzyme)
| Subtilizin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 3.4.21.62 | ||||||||
| CAS broj | 2598337 | ||||||||
| 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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Subtilizin (EC 3.4.21.62, alkalaza, alkalaza 0.6L, alkalaza 2.5L, ALK-enzim, bacilopeptidaza A, bacilopeptidaza B, Bacillus subtilis alkalna proteinaza biopraza, biopraza AL 15, biopraza APL 30, kolistinaza, subtilisin J, subtilisin S41, subtilisin Sendai, subtilisin GX, subtilisin E, subtilisin BL, genenaza I, esperaza, maksataza, alkalaza, termoaza PC 10, proteaza XXVII, termoaza, superaza, subtilisin DY, subtilopeptidaza, SP 266, savinaza 8.0L, savinaza 4.0T, kazusaza, proteaza VIII, optiklean, Bacillus subtilis alkalna proteinaza, protin A 3L, savinaza, savinaza 16.0L, savinaza 32.0 L EX, orientaza 10B, proteaza S) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Hidroliza proteina sa visokom specifičnošću za peptidne veze, sa preferencijom za veliki nepromenjeni ostatak i P1. Dolazi do hidrolize peptidnih amida
Subtilisin je serinska endopeptidaza.
Reference[uredi | uredi kod]
- ↑ Ottesen, M. and Svendsen, I. (1970). „The subtilisins”. Methods Enzymol. 19: 199-215.
- ↑ Markland, F.S. and Smith, E.L. (1971). „Subtilisins: primary structure, chemical and physical properties”. u: Boyer, P.D.. The Enzymes. 3 (3rd izd.). New York: Academic Press. str. 561-608.
- ↑ Philipp, M. and Bender, M.L. (1983). „Kinetics of subtilisin and thiolsubtilisin”. Mol. Cell. Biochem. 51: 5-32. PMID 6221910.
- ↑ Nedkov, P., Oberthür, W. and Braunitzer, G. (1985). „Determination of the complete amino acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN, Carlsberg and amylosacchariticus”. Biol. Chem. Hoppe-Seyler 366: 421-430. PMID 3927935.
- ↑ Ikemura, H., Takagi, H. and Inouye, M. (1987). „Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli”. J. Biol. Chem. 262: 7859-7864. PMID 3108260.
- ↑ Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.
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.
- Polgár, L. (1987). „Structure and function of serine proteases”. u: Neuberger, A. and Brocklehurst, K.. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. str. 159-200.
- Markland, F.S. and Smith, E.L. (1971). „Subtilisins: primary structure, chemical and physical properties”. u: Boyer, P.D.. The Enzymes. 3 (3rd izd.). New York: Academic Press. str. 561-608.