Site-directed mutagenesis on (serine) carboxypeptidase Y. A hydrogen bond network stabilizes the transition state by interaction with the C-terminal carboxylate group of the substrate

The three-dimensional structure of (serine) carboxypeptidase Y suggests that the side chains of Trp49, Asn51, Glu65, and Glu145 could be involved in the recognition of the C-terminal carboxylate group of peptide substrates. The mutations Trp49 to Phe; Asn51 to Ala, Asp, Glu, Gln, Ser, or Thr; Glu65...

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Veröffentlicht in:	Biochemistry (Easton) 1994-01, Vol.33 (2), p.508-517
Hauptverfasser:	Mortensen, Uffe H, Remington, S. James, Breddam, Klaus
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Analytical, structural and metabolic biochemistry Base Sequence Binding Sites Biological and medical sciences Carboxypeptidases - chemistry Carboxypeptidases - genetics Enzymes and enzyme inhibitors Esters - metabolism Fundamental and applied biological sciences. Psychology Glutamates - chemistry Glutamates - metabolism Glutamic Acid HIDROGENO Hydrogen Bonding Hydrogen-Ion Concentration HYDROGENE Hydrolases Hydrolysis Kinetics Molecular Sequence Data Molecular Structure MUTACION Mutagenesis, Site-Directed MUTATION PEPTIDASAS PEPTIDASE Peptides - metabolism SACCHAROMYCES CEREVISIAE Structure-Activity Relationship Substrate Specificity
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