<style face="normal" font="default" size="100%">Structural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum</style>

Drupal-Biblio

17

<style face="normal" font="default" size="100%">Structural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum</style>

Drupal-Biblio

17

<style face="normal" font="default" size="100%">Penicillin V acylase from pectobacterium atrosepticum exhibits high specific activity and unique kinetics</style>

Drupal-Biblio

17

<style face="normal" font="default" size="100%">Penicillin acylases revisited: importance beyond their industrial utility</style>

Drupal-Biblio

17

<style face="normal" font="default" size="100%">Structural analysis of a penicillin V acylase from pectobacterium atrosepticum confirms the importance of two Trp residues for activity and specificity</style>

Drupal-Biblio

17

<style face="normal" font="default" size="100%">Biotransformation of penicillin V to 6-aminopenicillanic acid using immobilized whole cells of E. coli expressing a highly active penicillin V acylase</style>