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Envelope-bound N-acetylmuramyl-L-alanine amidase of Escherichia coli K 12. Purification and properties of the enzyme.
van Heijenoort J, Parquet C, Flouret B, van Heijenoort Y. van Heijenoort J, et al. Eur J Biochem. 1975 Oct 15;58(2):611-9. doi: 10.1111/j.1432-1033.1975.tb02412.x. Eur J Biochem. 1975. PMID: 1102308 Free article.
N-Acetylmuramyl-L-alanine amidase activity was detected in Escherichia coli K 12 by usine N-acetylmuramyl-L-alanyl-gamma-D-glutamyl-(L)-meso-[3H]diaminopimelic acid as a radioactive substrate. This activity cleaves the amide bond between the residues o …
N-Acetylmuramyl-L-alanine amidase activity was detected in Escherichia coli K 12 by usine N-acetylmuramyl-L-alanyl-gamm …
N-acetylmuramoyl-L-alanine amidase of Escherichia coli K12. Possible physiological functions.
Parquet C, Flouret B, Leduc M, Hirota Y, van Heijenoort J. Parquet C, et al. Eur J Biochem. 1983 Jun 15;133(2):371-7. doi: 10.1111/j.1432-1033.1983.tb07472.x. Eur J Biochem. 1983. PMID: 6133749 Free article.
Various experiments were carried out in an attempt to determine the possible physiological function of the N-acetylmuramoyl-L-alanine amidase purified from Escherichia coli K12 on the basis of its activity on N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-di …
Various experiments were carried out in an attempt to determine the possible physiological function of the N-acetylmuramoyl-L-alan …
Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli.
Mengin-Lecreulx D, Flouret B, van Heijenoort J. Mengin-Lecreulx D, et al. J Bacteriol. 1982 Sep;151(3):1109-17. doi: 10.1128/jb.151.3.1109-1117.1982. J Bacteriol. 1982. PMID: 6125497 Free PMC article.
The enzymatic parameters of the four synthetases which catalyze the stepwise addition of L-alanine, D-glutamic acid, meso-diaminopimelic acid, and D-alanyl-D-alanine to uridine diphosphate-N-acetylmuramic acid were determined. ...Under the different in vitro …
The enzymatic parameters of the four synthetases which catalyze the stepwise addition of L-alanine, D-glutamic acid, meso-diam …
Crystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli.
Gordon E, Flouret B, Chantalat L, van Heijenoort J, Mengin-Lecreulx D, Dideberg O. Gordon E, et al. J Biol Chem. 2001 Apr 6;276(14):10999-1006. doi: 10.1074/jbc.M009835200. Epub 2000 Dec 20. J Biol Chem. 2001. PMID: 11124264 Free article.
UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptido …
UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-dia …
Carrier-mediated transport of pyroglutamyl-histidine in renal brush border membrane vesicles.
Skopicki HA, Fisher K, Zikos D, Flouret G, Bloch R, Kubillus S, Peterson DR. Skopicki HA, et al. Am J Physiol. 1988 Dec;255(6 Pt 1):C822-7. doi: 10.1152/ajpcell.1988.255.6.C822. Am J Physiol. 1988. PMID: 3202151
Transport of pGlu-His was not inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and N-beta-alanyl-L-histidine, which have been previously shown to be transported into renal brush border vesicles via a single, low-affinity, high-capacity, Na-independent, and H+- …
Transport of pGlu-His was not inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and N-beta-alanyl-L-histidine, which have …
Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli K12.
Michaud C, Blanot D, Flouret B, Van Heijenoort J. Michaud C, et al. Eur J Biochem. 1987 Aug 3;166(3):631-7. doi: 10.1111/j.1432-1033.1987.tb13560.x. Eur J Biochem. 1987. PMID: 3301347 Free article.
In order to investigate the specificity of these ligases, several compounds derived from their respective nucleotide substrates were prepared. In the case of the D-Glu-adding enzyme, DDP-MurNAc-L-Ala (DDP = dihydrouridine 5'-diphosphate) and P1-MurNAc-L-Ala were sub …
In order to investigate the specificity of these ligases, several compounds derived from their respective nucleotide substrates were prepare …
Organization of the murE-murG region of Escherichia coli: identification of the murD gene encoding the D-glutamic-acid-adding enzyme.
Mengin-Lecreulx D, Parquet C, Desviat LR, Plá J, Flouret B, Ayala JA, van Heijenoort J. Mengin-Lecreulx D, et al. J Bacteriol. 1989 Nov;171(11):6126-34. doi: 10.1128/jb.171.11.6126-6134.1989. J Bacteriol. 1989. PMID: 2681153 Free PMC article.
The 2-min region of the Escherichia coli genome contains a large cluster of genes from pbpB to envA that code for proteins involved in peptidoglycan biosynthesis and cell division. From pLC26-6 of the collection of Clarke and Carbon (L. Clarke and J. Carbon, Cell 9:91-99, …
The 2-min region of the Escherichia coli genome contains a large cluster of genes from pbpB to envA that code for proteins involved in pepti …