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

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...

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Published inBiochemistry (Easton) Vol. 39; no. 31; pp. 9430 - 9437
Main Authors Chang, Alan K, Nixon, Peter F, Duggleby, Ronald G
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 08.08.2000
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Abstract 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-terminal region must move aside to allow entry of the substrate, and again to permit the products to leave. Here we have examined the role of the carboxyl terminus by making 15 variants of the enzyme with serial deletions. The activity is largely unaffected by removal of up to seven residues but deletion of the next two, R561 and S560, results in a drastic loss of activity. Five of these deletion mutants were purified and fully characterized and showed progressive decreases in activity, in the ability to discriminate between pyruvate and larger substrates, and in cofactor affinity. Several substitution mutants at residues R561 and S560 were prepared, purified, and fully characterized. The results indicate important roles for the side-chain of R561 and the backbone atoms of S560. It is suggested that the carboxyl-terminal region of pyruvate decarboxylase is needed to lock in the cofactors and for the proper closure of the active site that is required for discrimination between substrates and for decarboxylation to occur.
AbstractList 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-terminal region must move aside to allow entry of the substrate, and again to permit the products to leave. Here we have examined the role of the carboxyl terminus by making 15 variants of the enzyme with serial deletions. The activity is largely unaffected by removal of up to seven residues but deletion of the next two, R561 and S560, results in a drastic loss of activity. Five of these deletion mutants were purified and fully characterized and showed progressive decreases in activity, in the ability to discriminate between pyruvate and larger substrates, and in cofactor affinity. Several substitution mutants at residues R561 and S560 were prepared, purified, and fully characterized. The results indicate important roles for the side-chain of R561 and the backbone atoms of S560. It is suggested that the carboxyl-terminal region of pyruvate decarboxylase is needed to lock in the cofactors and for the proper closure of the active site that is required for discrimination between substrates and for decarboxylation to occur.
Author Duggleby, Ronald G
Chang, Alan K
Nixon, Peter F
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Snippet The three-dimensional structure of Zymomonas mobilis pyruvate decarboxylase shows that the carboxyl-terminal region of the protein occludes the active site....
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StartPage 9430
SubjectTerms 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
Title Effects of Deletions at the Carboxyl Terminus of Zymomonas mobilis Pyruvate Decarboxylase on the Kinetic Properties and Substrate Specificity
URI http://dx.doi.org/10.1021/bi0002683
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