A. Pundle et H. Sivaraman, BACILLUS-SPHAERICUS PENICILLIN-V ACYLASE - PURIFICATION, SUBSTRATE-SPECIFICITY, AND ACTIVE-SITE CHARACTERIZATION, Current microbiology, 34(3), 1997, pp. 144-148
Penicillin V acylase from Bacillus sphaericus was purified to homogene
ity with an overall yield of 15%. The enzyme exhibited comparatively h
igh specificity for penicillin V, penicillin G, and other related comp
ounds being hydrolyzed at less than 10% of the rate of penicillin V. M
oreover, 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 indica
ted the involvement of lysine in the catalytic activity of the enzyme.