The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15 (Q27619119)

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M Nguyen-Distèche

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R Brasseur

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P Charlier

Journal of Biological Chemistry

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language of work or name

English

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publication date

30 July 1999

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published in

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volume

274

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issue

31

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page(s)

21853-60

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cites work

Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase

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Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein

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Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions

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Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors

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Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donors

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Methicillin-resistant staphylococci: detection methods and treatment of infections

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The mechanism of action of DD-peptidases: the role of Threonine-299 and -301 in the Streptomyces R61 DD-peptidase

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Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with beta-lactams

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Kinetic properties of the Bacillus licheniformis penicillin-binding proteins

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Serine beta-lactamases and penicillin-binding proteins

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Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution

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The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution

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Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution

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Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

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Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution

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TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant.

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Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis

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Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase

21 January 2018

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The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution

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X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

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Bioassay for carcinogenicity of rotenone in female Wistar rats.

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Effects of thiol reagents on Streptomyces K15 DD-peptidase-catalysed reactions

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SQUASH - combining constraints for macromolecular phase refinement and extension

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The hydrophobic moment detects periodicity in protein hydrophobicity

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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A standard numbering scheme for the class A beta-lactamases

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

21 January 2018

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Role of the conserved amino acids of the 'SDN' loop (Ser130, Asp131 and Asn132) in a class A beta-lactamase studied by site-directed mutagenesis

21 January 2018

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Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-binding DD-transpeptidase

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Molecular evolution of bacterial beta-lactam resistance

21 January 2018

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Arginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G beta-lactamase

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release_gi2v5raprfeabk5muiioxl6xxy

21 January 2018

Identifiers

DOI

10.1074/JBC.274.31.21853

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/gi2v5raprfeabk5muiioxl6xxy