Substrate specificity of immobilized penicillin-G acylase towards penicillin and cephalosporin derivatives was studied. The phenylacetyl moiety can be altered at the α-position with several small substituents. Depending on polarity and size of the substituent, enzyme activity decreases or increases. Insertion or deletion of atoms between the aromatic nucleus of the phenylacetyl group and the center of hydrolysis leads to substrates that are no longer recognized by the enzyme.
1994 ◽
Vol 4
(2)
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pp. 345-348
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2012 ◽
Vol 550-553
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pp. 1345-1351
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2016 ◽
Vol 46
(11)
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pp. 956-962
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1998 ◽
Vol 23
(5)
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pp. 305-310
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2000 ◽
Vol 18
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pp. 253-258
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2017 ◽
Vol 28
(1)
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pp. 146-152
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2013 ◽
Vol 74
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pp. 88-94
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2008 ◽
Vol 114
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pp. 507-510
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