Effects of Deletions at the Carboxyl Terminus of Zymomonas mobilis Pyruvate Decarboxylase on the Kinetic Properties and Substrate Specificity

• Published in: Biochemistry (Easton) Vol. 39; no. 31; pp. 9430 - 9437
• Main Authors: Chang, Alan K, Nixon, Peter F, Duggleby, Ronald G
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 08.08.2000
• Subjects: Amino Acid Sequence; Amino Acid Substitution - genetics; Arginine - genetics; Binding Sites - genetics; Coenzymes - metabolism; Enzyme Activation - genetics; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments - genetics; Peptide Fragments - metabolism; Pyruvate Decarboxylase - genetics; Pyruvate Decarboxylase - metabolism; Sequence Deletion; Serine - genetics; Substrate Specificity - genetics; Zymomonas - enzymology; Zymomonas - metabolism; Zymomonas mobilis

The three-dimensional structure of Zymomonas mobilis pyruvate decarboxylase shows that the carboxyl-terminal region of the protein occludes the active site. This observation is consistent with earlier suggestions that the active site is inaccessible to solvent during catalysis. However, the carboxyl...