Mandelonitrilna lijaza
(Preusmjereno sa stranice PaHNL)
Mandelonitrilna lijaza (EC 4.1.2.10, (R)-oksinitrilaza, oksinitrilaza, D-oksinitrilaza, D-alfa-hidroksinitril lijaza, mandelonitril benzaldehid-lijaza, PaHNL, AtHNL, PhaMDL, (R)-HNL, (R)-PeHNL, (R)-hidroksinitril lijaza, R-selektivna hidroksinitrilna lijaza, R-selektivna HNL, (R)-(+)-mandelonitrilna lijaza) je enzim sa sistematskim imenom (R)-mandelonitril benzaldehid-lijaza (formira cijanid).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Mandelonitrilna lijaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 4.1.2.10 | ||||||||
CAS broj | 9024-43-5 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
- (R)-mandelonitril cijanid + benzaldehid
Ova enzimska klasa obuhvata raznovrsne enzime iz različitih izvora.
Reference
uredi- ↑ Ueatrongchit, T., Kayo, A., Komeda, H., Asano, Y. and H-Kittikun, A. (2008). „Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat)”. Biosci. Biotechnol. Biochem. 72: 1513-1522. PMID 18540101.
- ↑ Lin, G., Han, S. and Li, Z. (1999). „Enzymic synthesis of (R)-cyanohydrins by three (R)-oxynitrilase sources in micro-aqueous organic medium”. Tetrahedron 55: 3531-3540.
- ↑ de Gonzalo, G., Brieva, R. and Gotor, V. (2002). „(R)-Oxynitrilase-catalyzed transformation of ω-hydroxyalkanals”. J. Mol. Catal. B 19-20: 223-230.
- ↑ Ueatrongchit, T., Tamura, K., Ohmiya, T., H-Kittikun, A. and Asano, Y. (2010). „Hydroxynitrile lyase from Passiflora edulis. Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile”. Enzyme Microb. Technol. 46: 456-465.
- ↑ Andexer, J., von Langermann, J., Mell, A., Bocola, M., Kragl, U., Eggert, T. and Pohl, M. (2007). „An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an α/β-hydrolase fold”. Angew. Chem. Int. Ed. Engl. 46: 8679-8681. PMID 17907254.
- ↑ Guterl, J.K., Andexer, J.N., Sehl, T., von Langermann, J., Frindi-Wosch, I., Rosenkranz, T., Fitter, J., Gruber, K., Kragl, U., Eggert, T. and Pohl, M. (2009). „Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with α/β-hydrolase fold”. J. Biotechnol. 141: 166-173. PMID 19433222.
Literatura
uredi- 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.