Bacillus sphaericus penicillin V acylase: purification, substrate specificity, and active-site characterization.
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.
Pundle
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Division of Biochemical Sciences, National Chemical Laboratory, Pune 411 008, India.
SivaRaman
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H
D001407:Bacillus / Q000201:enzymology*; D001665:Binding Sites; D010399:Penicillin Amidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D010399:Penicillin Amidase