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Model catalysts which simulate penicillinase I. Effect of ionic interaction on catalysis of penicillin hydrolysis by certain catecholamines

โœ Scribed by Michael A. Schwartz

Publisher
John Wiley and Sons
Year
1965
Tongue
English
Weight
391 KB
Volume
54
Category
Article
ISSN
0022-3549

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โœฆ Synopsis

Further studies on the nature of the catalysis of hydrolysis of penicillin G by 3,6-bis-(dimethylaminomethy1)catechol (CDM) show that the active species of this compound (+ 1 charge) interacts by electrostatic attraction with the negatively charged penicillin. The 3,5-substituted catechol shows no H of maximum rate, as does CDM, and much lower catalytic rate, indicating that foth aminomethyl groups must be ortho to the hydroxyl groups for maximum catalytic effect. The possible relationships of CDM to the enzyme penicillinase are discussed.

T IS OFTEN proposed that the high catalytic

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