Horizmatna sintaza
Horizmatna sintaza | |||||||||
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Horizmatna sintaza homotetramer, Streptococcus pneumoniae | |||||||||
Identifikatori | |||||||||
EC broj | 4.2.3.5 | ||||||||
CAS broj | 9077-07-0 | ||||||||
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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Horizmatna sintaza (EC 4.2.3.5, 5-O-(1-karboksivinil)-3-fosfošikimat fosfat-lijaza) je enzim sa sistematskim imenom 5-O-(1-karboksivinil)-3-fosfošikimat fosfat-lijaza (formira horizmat).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 5-O-(1-karboksivinil)-3-fosfošikimat horizmat + fosfat
Za dejstvo ovog enzima je neophodan FMN.
Reference
- ↑ Gaertner, F.H. and Cole, K.W. (1973). „Properties of chorismate synthase in Neurospora crassa”. J. Biol. Chem. 248: 4602-4609. PMID 4146266.
- ↑ Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. (1967). „The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate”. J. Biol. Chem. 242: 82-90. PMID 4289188.
- ↑ Welch, G.R., Cole, K.W. and Gaertner, F.H. (1974). „Chorismate synthase of Neurospora crassa: a flavoprotein”. Arch. Biochem. Biophys. 165: 505-518. PMID 4155270.
- ↑ Bornemann, S., Lowe, D.J. and Thorneley, R.N. (1996). „The transient kinetics of Escherichia coli chorismate synthase: substrate consumption, product formation, phosphate dissociation, and characterization of a flavin intermediate”. Biochemistry 35: 9907-9916. PMID 8703965.
- ↑ Bornemann, S., Theoclitou, M.E., Brune, M., Webb, M.R., Thorneley, R.N. and Abell, C. (2000). „A secondary β deuterium kinetic isotope effect in the chorismate synthase reaction”. Bioorg. Chem. 28: 191-204. PMID 11034781.
- ↑ Osborne, A., Thorneley, R.N., Abell, C. and Bornemann, S. (2000). „Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction”. J. Biol. Chem. 275: 35825-35830. PMID 10956653.
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 Chorismate+synthase
- 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