The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00186a042
Reference24 articles.
1. The Glu residue in the conserved ASN-Glu-Pro sequence of two highly divergent endo-β-1,4-glucanases is essential for enzymatic activity
2. Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-β-1,4-glucanase and β-1,4-xylanase from the bacterium Cellulomonas fimi
3. MOLECULAR BIOLOGY OF CELLULOSE DEGRADATION
4. Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
5. Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli.
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