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Cover Picture: ChemBioChem 9/2002
Author(s) -
Brik Ashraf,
D'Souza Lawrence J.,
Keinan Ehud,
Grynszpan Flavio,
Dawson Philip E.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020902)3:9<799::aid-cbic799>3.0.co;2-7
Subject(s) - chemistry , tautomer , decarboxylation , bifunctional , nucleophile , stereochemistry , mutant , combinatorial chemistry , catalysis , biochemistry , gene
The cover picture shows a schematic representation of the mechanistic and catalytic diversity exhibited by mutants of 4‐oxalocrotonate tautomerase (4‐OT). A designed single amino acid substitution can alter the catalytic activity and mechanism of this enzyme. While the wild‐type 4‐OT catalyzes only the tautomerization of oxalocrotonate through a general acid/base machanism, the Pro1Ala mutant catalyzes two reactions—the original tautomerization reaction through an acid/base mechanism and the decarboxylation of oxaloacetate by a nucleophilic mechanism. This bifunctional mutant suggests that a new synthetic family of nucleophilic catalysts could be generated on the basis of the 4‐OT scaffold through selection methods and rational protein engineering. For more details, see the article by Brik et al. on p. 845 ff.