Antranilat fosforiboziltransferaza
| Antranilat fosforiboziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Antranilat fosforiboziltransferaza homodimer, Mycobacterium tuberculosis | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.4.2.18 | ||||||||
| CAS broj | 9059-35-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Antranilat fosforiboziltransferaza (EC 2.4.2.18, fosforibozil-antranilat pirofosforilaza, PRT, antranilat 5-fosforibozilpirofosfat fosforiboziltransferaza, antranilat fosforibozilpirofosfat fosforiboziltransferaza, fosforibozilantranilat pirofosforilaza, fosforibozilantranilat transferaza, antranilat-PP-riboza-P fosforiboziltransferaza) je enzim sa sistematskim imenom N-(5-fosfo-D-ribozil)-antranilat:difosfat fosfo-alfa-D-riboziltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- N-(5-fosfo-D-ribozil)-antranilat + difosfat antranilat + 5-fosfo-alfa-D-riboza 1-difosfat
Kod pojedinih organizama, ovaj enzim je deo multifunkcionalnog proteina zajedno sa jednom ili više komponenti sistema za biosintezu triptofana, cf. EC 4.1.1.48 (indol-3-glicerol-fosfat sintaza), EC 4.1.3.27 (antranilat sintaza), EC 4.2.1.20 (triptofan sintaza) i EC 5.3.1.24 (fosforibozilantranilat izomeraza).
Reference
- ↑ Creighton, T.E. and Yanofsky, C. (1970). „Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase”. Methods Enzymol. 17A: 365-380.
- ↑ Hütter, R., Niederberger, P. and DeMoss, J.A. (1986). „Tryptophan synthetic genes in eukaryotic microorganisms”. Annu. Rev. Microbiol. 40: 55-77. PMID 3535653.
- ↑ Ito, J. and Yanofsky, C. (1969). „Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits”. J. Bacteriol. 97: 734-742. PMID 4886290.
- ↑ Wegman, J. and DeMoss, J.A. (1965). „The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa”. J. Biol. Chem. 240: 3781-3788. PMID 5842052.
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.
Vanjske veze
- MeSH Anthranilate+phosphoribosyltransferase
- 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
