UDP-N-acetilglukozamin difosforilaza
| UDP-N-acetilglukozamin difosforilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.7.23 | ||||||||
| CAS broj | 2601781 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
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
[уреди | уреди извор]- ^ Pattabiramin, T.N. & Bachhawat, B.K. (1961). „Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain”. Biochim. Biophys. Acta. 50: 129—134. PMID 13733356.
- ^ Strominger, J.L. & Smith, M.S. (1959). „Uridine diphosphoacetylglucosamine pyrophosphorylase”. J. Biol. Chem. 234: 1822—1827. PMID 13672971.
- ^ Mengin-Lecreulx, D. & 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. & 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- UDP-N-acetylglucosamine+diphosphorylase на US National Library of Medicine Medical Subject Headings (MeSH)
