UDP-N-acetilglukozamin difosforilaza
| UDP-N-acetilglukozamin difosforilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| UDP-N-acetilglukozamin difosforilaza homotrimer, Mycobacterium tuberculosis | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.7.23 | ||||||||
| CAS broj | 2601781 | ||||||||
| 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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UDP-N-acetilglukozamin difosforilaza (EC 2.7.7.23, UDP-N-acetilglukozamin pirofosforilaza, uridin difosfoacetilglukozamin pirofosforilaza, UTP:2-acetamido-2-dezoksi-alfa-D-glukoza-1-fosfat uridililtransferaza, UDP-GlcNAc pirofosforilaza, GlmU uridililtransferaza, acetilglukozamin 1-fosfat uridililtransferaza, UDP-acetilglukozamin pirofosforilaza, uridin difosfat-N-acetilglukozamin pirofosforilaza, uridin difosfoacetilglukozamin fosforilaza, acetilglukozamin 1-fosfat uridililtransferaza) je enzim sa sistematskim imenom UTP:N-acetil-alfa-D-glukozamin-1-fosfat uridililtransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- UTP + N-acetil-alfa-D-glukozamin 1-fosfat difosfat + UDP-N-acetil-alfa-D-glukozamin
Ovaj enzim učestvuje u biosintezi acetamido šećera kod bakterija i arheja.
Reference
- ↑ Pattabiramin, T.N. and Bachhawat, B.K. (1961). „Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain”. Biochim. Biophys. Acta 50: 129-134. PMID 13733356.
- ↑ Strominger, J.L. and Smith, M.S. (1959). „Uridine diphosphoacetylglucosamine pyrophosphorylase”. J. Biol. Chem. 234: 1822-1827. PMID 13672971.
- ↑ Mengin-Lecreulx, D. and van Heijenoort, J. (1994). „Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis”. J. Bacteriol. 176: 5788-5795. PMID 8083170.
- ↑ Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. (1996). „Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli”. Biochemistry 35: 579-585. PMID 8555230.
- ↑ Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. (1998). „A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc”. J. Biol. Chem. 273: 27055-27057. PMID 9765219.
- ↑ Olsen, L.R. and Roderick, S.L. (2001). „Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites”. Biochemistry 40: 1913-1921. PMID 11329257.
- ↑ Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. (2001). „Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture”. EMBO J. 20: 6191-6202. PMID 11707391.
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 UDP-N-acetylglucosamine+diphosphorylase
- 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
