Abstract
Of four enzymatically active forms of Alcaligenes faecalis penicillin amidase (EC 3.5.1.11) observed in sonicated cells, two (PA5.5 and PA5.3; subscript denotes pI) could be isolated and purified in two steps from the cells destroyed by osmotic shock. Active enzyme was only found in the periplasm. PA5.5 converts further to PA5.3 which differs in the molecular mass of the A-chain. The origin of these differences is a conversion of the N-terminal Gln to pyrolideno-carboxilic acid and a loss of three amino acids from the C-terminus of the A-chain. PA5.3 had higher specific activity (10–30%) for the hydrolysis of benzylpenicillin and 6-nitro-3-phenylacetamidobenzoic acid than PA5.5. © Rapid Science Ltd. 1998
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
