Feruloilna estaraza
Feruloilna estaraza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.1.1.73 | ||||||||
CAS broj | 134712-49-5 | ||||||||
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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Feruloilna estaraza (EC 3.1.1.73, ferulinsko kiselinska esteraza, hidroksicinamoilna esteraza, hemicelulazno pristupni enzim, FAE-III, cinamoil estarska hidrolaza, FAEA, cinnAE, FAE-I, FAE-II) je enzim sa sistematskim imenom 4-hidroksi-3-metoksicinamoil-šećer hidrolaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- feruloil-polisaharid + H2O ferulat + polisaharid
Ovaj enzim katalizuje hidrolizu 4-hidroksi-3-metoksicinamoil (feruloil) grupa u estarifikovanim šećerima.
Reference
- ↑ Faulds, C.B. and Williamson, G. (1991). „The purification and characterisation of 4-hydroxy-3-methoxy-cinnamic (ferulic) acid esterase from Streptomyces olivochromogenes (3232)”. J. Gen. Microbiol. 137: 2339-2345. PMID 1663152.
- ↑ Faulds, C.B. and Williamson, G. (1994). „Purification and characterisation of a ferulic acid esterase (FAE-III) from Aspergillus niger. Specificity for the phenolic moiety and binding to microcrystalline cellulose”. Microbiology 140: 779-787.
- ↑ Kroon, P.A., Faulds, C.B. and Williamson, G. (1996). „Purification and characterisation of a novel ferulic acid esterase induced by growth of Aspergillus niger on sugarbeet pulp”. Biotechnol. Appl. Biochem. 23: 255-262. PMID 8679110.
- ↑ deVries, R.P. (1997). „, Michelsen,B., Poulsen, C.H., Kroon, P.A., van den Heuvel, R.H.H., Faulds, C.B., Williamson, G., van den Homberg, J.P.T.W. and Visser, J. The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides”. Appl. Environ. Microbiol. 63: 4638-4644. PMID 9406381.
- ↑ Castanares, A., Mccrae, S.I. and Wood, T.M. (1992). „Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum”. Enzyme Microbiol. Technol. 14: 875-884.
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.
Spoljašnje veze
- MeSH Feruloyl+esterase
- 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