Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
about
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent.Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae.Amino acid sequence of the penicillin-binding protein/DD-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A.Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues.Knockout of the two ldh genes has a major impact on peptidoglycan precursor synthesis in Lactobacillus plantarum.The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate.Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteinsEffects of thiol reagents on Streptomyces K15 DD-peptidase-catalysed reactions.The Streptomyces K15 DD-peptidase/penicillin-binding protein. Active site and sequence of the N-terminal region.Evidence from a mutant beta-lactamase for the mechanism of beta-lactamase-catalysed depsipeptide aminolysis.Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein.On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptidesActive-site and membrane topology of the DD-peptidase/penicillin-binding protein no. 6 of Enterococcus hirae (Streptococcus faecium) A.T.C.C. 9790.Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donorsThe pH dependence of the active-site serine DD-peptidase of Streptomyces R61.Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions
P2860
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P2860
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@en
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@nl
type
label
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@en
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@nl
prefLabel
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@en
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@nl
P2093
P2860
P356
P1433
P1476
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
@en
P2093
Ghuysen JM
Leyh-Bouille M
Nguyen-Distèche M
P2860
P304
P356
10.1042/BJ2350167
P407
P577
1986-04-01T00:00:00Z