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Crystal structure of penicillin G acylase from the bro1 mutant strain of providencia rettgeri
Penicillin G acylase is an important enzyme in the commercial production of semisynthetic penicillins used to combat bacterial infections. Mutant strains of Providencia rettgeri were generated fromExpand
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The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.
Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2Expand
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On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.
Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase fromExpand
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X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme
Hen egg white lysozyme was the first enzyme whose structure was determined by X-ray crystallography1. The proposed mechanism2–4 based on this structure involves the distortion of the saccharideExpand
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2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams.
The crystallographic structure of the penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 has been solved to 2.8-A resolution. The 38,000-dalton serine peptidase hasExpand
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Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins.
The sequences of class A beta-lactamases were compared. Four main groups of enzymes were distinguished: those from the gram-negative organisms and bacilli and two distinct groups of Streptomyces spp.Expand
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Crystallographic mapping of beta-lactams bound to a D-alanyl-D-alanine peptidase target enzyme.
X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target ofExpand
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Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins.
Penicillin-binding proteins (PBPs), the target enzymes of beta-lactam antibiotics such as penicillins and cephalosporins, catalyze the final peptidoglycan cross-linking step of bacterial cell-wallExpand
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Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin".
The bacterial D-alanyl-D-alanine transpeptidases (DD-peptidases) are the killing targets of beta-lactams, the most important clinical defense against bacterial infections. However, due to theExpand
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