UDP-N-acetilglukozamin difosforilaza

UDP-N-acetilglukozamin difosforilaza
Identifikatori
EC broj2.7.7.23
CAS broj2601781
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum
Pretraga
PMCčlanci
PubMedčlanci
NCBIproteini

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 {\displaystyle \rightleftharpoons } difosfat + UDP-N-acetil-alfa-D-glukozamin

Ovaj enzim učestvuje u biosintezi acetamido šećera kod bakterija i arheja.

Reference

  1. ^ Pattabiramin, T.N. & Bachhawat, B.K. (1961). „Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain”. Biochim. Biophys. Acta. 50: 129—134. PMID 13733356. 
  2. ^ Strominger, J.L. & Smith, M.S. (1959). „Uridine diphosphoacetylglucosamine pyrophosphorylase”. J. Biol. Chem. 234: 1822—1827. PMID 13672971. 
  3. ^ 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. 
  4. ^ 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  5. ^ 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  6. ^ Olsen, L.R. & Roderick, S.L. (2001). „Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites”. Biochemistry. 40: 1913—1921. PMID 11329257. 
  7. ^ 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)

Literatura

  • 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

  • UDP-N-acetylglucosamine+diphosphorylase на US National Library of Medicine Medical Subject Headings (MeSH)
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