Pages that link to "Q37735680"
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The following pages link to Altering enzymatic activity: recruitment of carboxypeptidase activity into an RTEM beta-lactamase/penicillin-binding protein 5 chimera (Q37735680):
Displaying 8 items.
- Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases (Q27936010) (← links)
- A suicide-substrate mechanism for hydrolysis of beta-lactams by an anti-idiotypic catalytic antibody. (Q32078469) (← links)
- Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli. (Q34810275) (← links)
- Critical amino acids responsible for converting specificities of proteins and for enhancing enzyme evolution are located around beta-turn potentials: data-based prediction (Q36745396) (← links)
- Recovery of active beta-lactamases from Proteus vulgaris and RTEM-1 hybrid by random mutagenesis by using a dnaQ strain of Escherichia coli (Q39782787) (← links)
- Common beta-lactamases inhibit bacterial biofilm formation (Q42736090) (← links)
- Molecular Basis of Substrate Recognition and Product Release by the Klebsiella pneumoniae Carbapenemase (KPC-2). (Q48304942) (← links)
- Antibacterial Spectrum of a Tetrazole-Based Reversible Inhibitor of Serine β-Lactamases (Q57174339) (← links)