These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
184 related articles for article (PubMed ID: 15531591)
1. Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. Eschenburg S; Priestman M; Schönbrunn E J Biol Chem; 2005 Feb; 280(5):3757-63. PubMed ID: 15531591 [TBL] [Abstract][Full Text] [Related]
2. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Skarzynski T; Mistry A; Wonacott A; Hutchinson SE; Kelly VA; Duncan K Structure; 1996 Dec; 4(12):1465-74. PubMed ID: 8994972 [TBL] [Abstract][Full Text] [Related]
3. Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin. Samland AK; Amrhein N; Macheroux P Biochemistry; 1999 Oct; 38(40):13162-9. PubMed ID: 10529188 [TBL] [Abstract][Full Text] [Related]
4. Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae. Samland AK; Etezady-Esfarjani T; Amrhein N; Macheroux P Biochemistry; 2001 Feb; 40(6):1550-9. PubMed ID: 11327813 [TBL] [Abstract][Full Text] [Related]
5. A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA). Eschenburg S; Priestman MA; Abdul-Latif FA; Delachaume C; Fassy F; Schönbrunn E J Biol Chem; 2005 Apr; 280(14):14070-5. PubMed ID: 15701635 [TBL] [Abstract][Full Text] [Related]
6. Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin. Kim DH; Lees WJ; Kempsell KE; Lane WS; Duncan K; Walsh CT Biochemistry; 1996 Apr; 35(15):4923-8. PubMed ID: 8664284 [TBL] [Abstract][Full Text] [Related]
7. Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA. Schönbrunn E; Eschenburg S; Krekel F; Luger K; Amrhein N Biochemistry; 2000 Mar; 39(9):2164-73. PubMed ID: 10694381 [TBL] [Abstract][Full Text] [Related]
8. Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase) from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Bensen DC; Rodriguez S; Nix J; Cunningham ML; Tari LW Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Apr; 68(Pt 4):382-5. PubMed ID: 22505403 [TBL] [Abstract][Full Text] [Related]
9. In vitro and in vivo functional activity of Chlamydia MurA, a UDP-N-acetylglucosamine enolpyruvyl transferase involved in peptidoglycan synthesis and fosfomycin resistance. McCoy AJ; Sandlin RC; Maurelli AT J Bacteriol; 2003 Feb; 185(4):1218-28. PubMed ID: 12562791 [TBL] [Abstract][Full Text] [Related]
10. Evidence of kinetic control of ligand binding and staged product release in MurA (enolpyruvyl UDP-GlcNAc synthase)-catalyzed reactions . Jackson SG; Zhang F; Chindemi P; Junop MS; Berti PJ Biochemistry; 2009 Dec; 48(49):11715-23. PubMed ID: 19899805 [TBL] [Abstract][Full Text] [Related]
11. A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. Eschenburg S; Kabsch W; Healy ML; Schonbrunn E J Biol Chem; 2003 Dec; 278(49):49215-22. PubMed ID: 13129913 [TBL] [Abstract][Full Text] [Related]
12. The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) . Han H; Yang Y; Olesen SH; Becker A; Betzi S; Schönbrunn E Biochemistry; 2010 May; 49(19):4276-82. PubMed ID: 20392080 [TBL] [Abstract][Full Text] [Related]
13. Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA). Zhu JY; Yang Y; Han H; Betzi S; Olesen SH; Marsilio F; Schönbrunn E J Biol Chem; 2012 Apr; 287(16):12657-67. PubMed ID: 22378791 [TBL] [Abstract][Full Text] [Related]
14. Determination of the pKa value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae. Krekel F; Samland AK; Macheroux P; Amrhein N; Evans JN Biochemistry; 2000 Oct; 39(41):12671-7. PubMed ID: 11027147 [TBL] [Abstract][Full Text] [Related]
15. Identification of a novel UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Vibrio fischeri that confers high fosfomycin resistance in Escherichia coli. Kumar S; Parvathi A; Hernandez RL; Cadle KM; Varela MF Arch Microbiol; 2009 May; 191(5):425-9. PubMed ID: 19277606 [TBL] [Abstract][Full Text] [Related]
16. Evidence that the reaction of the UDP-N-acetylglucosamine 1-carboxyvinyltransferase proceeds through the O-phosphothioketal of pyruvic acid bound to Cys115 of the enzyme. Wanke C; Amrhein N Eur J Biochem; 1993 Dec; 218(3):861-70. PubMed ID: 8281938 [TBL] [Abstract][Full Text] [Related]
17. Advances in UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) Covalent Inhibition. de Oliveira MVD; Furtado RM; da Costa KS; Vakal S; Lima AH Front Mol Biosci; 2022; 9():889825. PubMed ID: 35936791 [TBL] [Abstract][Full Text] [Related]
18. Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Skarzynski T; Kim DH; Lees WJ; Walsh CT; Duncan K Biochemistry; 1998 Feb; 37(8):2572-7. PubMed ID: 9485407 [TBL] [Abstract][Full Text] [Related]
19. Lyme disease enolpyruvyl-UDP-GlcNAc synthase: fosfomycin-resistant MurA from Borrelia burgdorferi, a fosfomycin-sensitive mutant, and the catalytic role of the active site Asp. Jiang S; Gilpin ME; Attia M; Ting YL; Berti PJ Biochemistry; 2011 Mar; 50(12):2205-12. PubMed ID: 21294548 [TBL] [Abstract][Full Text] [Related]
20. Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enolpyruvyl transferase. Thomas AM; Ginj C; Jelesarov I; Amrhein N; Macheroux P Eur J Biochem; 2004 Jul; 271(13):2682-90. PubMed ID: 15206933 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]