SUBSTRATE-SPECIFICITY OF IMMOBILIZED PENICILLIN-G ACYLASE

Authors
VANDERMEY M DEVROOM E
Citation
M. Vandermey et E. Devroom, SUBSTRATE-SPECIFICITY OF IMMOBILIZED PENICILLIN-G ACYLASE, Bioorganic & medicinal chemistry letters, 4(2), 1994, pp. 345-348
Citations number
17
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
4
Issue
2
Year of publication
1994
Pages
345 - 348
Database
ISI
SICI code
0960-894X(1994)4:2<345:SOIPA>2.0.ZU;2-6
Abstract
The substrate specificity of immobilized penicillin-Ci acylase towards penicillin and cephalosporin derivatives was studied. The phenylacety l moiety can be altered at the a-position with several small substitue nts. Depending on polarity and size of the substituent, enzyme activit y decreases or increases. Insertion or deletion of atoms between the a romatic nucleus of the phenylacetyl group and the center of hydrolysis leads to substrates that are no longer recognized by the enzyme.