PMID: 9009066Mar 1, 1997Paper

Bacillus sphaericus penicillin V acylase: purification, substrate specificity, and active-site characterization

Current Microbiology
A V Pundle, H SivaRaman

Abstract

Penicillin V acylase from Bacillus sphaericus was purified to homogeneity with an overall yield of 15%. The enzyme exhibited comparatively high specificity for penicillin V, penicillin G, and other related compounds being hydrolyzed at less than 10% of the rate of penicillin V. Moreover, the high rate of hydrolysis was observed when the side chain of the substrate molecule was unsubstituted. Lysine-modifying reagents inactivated the enzyme rapidly. Kinetics and titration studies indicated the involvement of lysine in the catalytic activity of the enzyme.

Citations

Mar 2, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·P Manish ChandraC G Suresh
Nov 29, 2014·Critical Reviews in Biotechnology·Vellore Sunder AvinashCheravakkattu Gopalan Suresh
Oct 13, 2009·Journal of Photochemistry and Photobiology. B, Biology·Atul KumarArchana Pundle
Jul 16, 2013·Biochemical and Biophysical Research Communications·V S AvinashSureshkumar Ramasamy
Oct 23, 2016·Biochimica Et Biophysica Acta. General Subjects·Deepak ChandSureshkumar Ramasamy
Apr 4, 2021·Microorganisms·Jack W DalyCormac G M Gahan

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