3-Dehidrohinatna sintaza
| 3-dehidrohinatna sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 4.2.3.4 | ||||||||
| CAS broj | 37211-77-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
3-dehidrohinatna sintaza (EC 4.2.3.4, 5-dehidrohinat sintaza, 5-dehidrohinatno kiselinska sintetaza, dehidrohinatna sintaza, 3-dehidrohinatna sintetaza, 3-dezoksi-arabino-heptulozonat-7-fosfat fosfat-lijaza (ciklizacija), 3-dezoksi-arabino-heptulonat-7-fosfat fosfat-lijaza (ciklizacija), 3-dezoksi-arabino-heptulonat-7-fosfat fosfat-lijaza (ciklizacija, formira 3-dehidrohinat)) je enzim sa sistematskim imenom 3-dezoksi-D-arabino-hept-2-ulosonat-7-fosfat fosfat-lijaza (ciklizacija, formira 3-dehidrohinat).[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 3-dezoksi-D-arabino-hept-2-ulosonat 7-fosfat 3-dehidrohinat + fosfat
Za dejstvo ovog enzima je neophodan jon Co2+ i vezani NAD+.
Reference
- ↑ Rotenberg, S.L. and Sprinson, D.B. (1970). „Mechanism and stereochemistry of 5-dehydroquinate synthetase”. Proc. Natl. Acad. Sci. USA 67: 1669-1672. PMID 5275368.
- ↑ Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. (1963). „The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate”. J. Biol. Chem. 238: 3176-3182. PMID 14085358.
- ↑ Bender, S.L., Mehdi, S. and Knowles, J.R. (1989). „Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis”. Biochemistry 28: 7555-7560. PMID 2514789.
- ↑ Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. (1998). „Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis”. Nature 394: 299-302. PMID 9685163.
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 3-dehydroquinate+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
