UDP-N-acetilglukozamin—undekaprenil-fosfat N-acetilglukozaminfosfotransferaza

UDP-N-acetilglukozamin—undekaprenil-fosfat N-acetilglukozaminfosfotransferaza
Identifikatori
EC broj 2.7.8.33
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search

UDP-N-acetilglukozamin—undekaprenil-fosfat N-acetilglukozaminfosfotransferaza (EC 2.7.8.33, UDP-N-acetilglukozamin:undekaprenil-fosfat GlcNAc-1-fosfat transferaza, WecA, WecA transferaza, UDP-GIcNAc:undekaprenil fosfat N-acetilglukozaminil 1-P transferaza, GlcNAc-P-P-Und sintaza, GPT, TagO, UDP-GlcNAc:undekaprenil-fosfat GlcNAc-1-fosfat transferaza, UDP-N-acetil-D-glukozamin:ditrans,oktacis-undekaprenil fosfat N-acetilglukozaminfosfotransferaza) je enzim sa sistematskim imenom UDP-N-acetil-alfa-D-glukozamin:ditrans,oktacis-undekaprenil fosfat N-acetil-alfa-D-glukozaminfosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

UDP-N-acetil-alfa-D-glukozamin + ditrans,oktacis-undekaprenil fosfat ⇌ {\displaystyle \rightleftharpoons } UMP + N-acetil-alfa-D-glukozaminildifosfo-ditrans,oktacis-undekaprenol

Ovaj enzim katalizuje sintezu ditrans,oktacis-undekaprenil-N-acetil-alfa-D-glukozaminil difosfata.

Reference

  1. ↑ Al-Dabbagh, B., Mengin-Lecreulx, D. and Bouhss, A. (2008). „Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA”. J. Bacteriol. 190: 7141-7146. PMID 18723618. 
  2. ↑ Lehrer, J., Vigeant, K.A., Tatar, L.D. and Valvano, M.A. (2007). „Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide”. J. Bacteriol. 189: 2618-2628. PMID 17237164. 
  3. ↑ Rush, J.S., Rick, P.D. and Waechter, C.J. (1997). „Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli”. Glycobiology 7: 315-322. PMID 9134438. 
  4. ↑ Soldo, B., Lazarevic, V. and Karamata, D. (2002). „tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168”. Microbiology 148: 2079-2087. PMID 12101296. 

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---undecaprenyl-phosphate+N-acetylglucosaminephosphotransferase
  • p
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Proteini: enzimi
Teme
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
Tipovi
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