PhanerochaeteV1, Main, Exploration, bibRecord, 000245

Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.

Identifieur interne : 000245 ( Main/Exploration ); précédent : 000244; suivant : 000246

Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.

Auteurs : Zhixin Jing [République populaire de Chine] ; Hong Feng

Source :

The protein journal [ 1875-8355 ] ; 2015.

RBID : pubmed:25957260

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (chemistry), Amino Acids (metabolism), Aminopeptidases (chemistry), Aminopeptidases (genetics), Aminopeptidases (metabolism), Enzyme Stability (MeSH), Escherichia coli (genetics), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Molecular Docking Simulation (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
MESH :
- chemical , chemistry : Amino Acids, Aminopeptidases, Fungal Proteins, Recombinant Proteins.
- chemical , genetics : Aminopeptidases, Fungal Proteins, Recombinant Proteins.
- chemical , metabolism : Amino Acids, Aminopeptidases, Fungal Proteins, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Escherichia coli, Phanerochaete.
- Amino Acid Sequence, Enzyme Stability, Molecular Docking Simulation, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Sequence Alignment, Substrate Specificity.

Abstract

The proline iminopeptidase (PchPiPA) of Phanerochaete chrysosporium catalyze specifically hydrolysis of N-terminal proline from peptides. The substrate Pro-pNA was docked into the catalytic pocket and several amino acid residues were identified to interact or associate with the substrate. Eight residues were selected for site-directed mutagenesis. The wild-type and mutant proteins were expressed in Escherichia coli and purified. Kinetic parameters were calculated by hydrolyzing Pro-pNA for these enzymes. Substitution of two Glu residues (Glu198 and Glu227) which interact with the substrate via formation of hydrogen bond, led to deleterious effect on catalytic efficiency (k(cat)/K(m)) due to decrease of k(cat) and increase of K(m). Four Phe residues consisting of catalytic pocket and surrounding the docked substrate, were substituted with Ala, resulting in decrease in k(cat)/K(m) to various extents. Substitution of two residues (Val267 and Cys267) localized at the deep end of the catalytic pocket also yielded negative influence on the substrate hydrolysis. Besides, all the mutants except E227Q exhibited lower thermostability than the wild-type did, indicating that these mutations may modulate the local structure. In conclusion, these amino acid residues may play an important role in maintaining local environment of the impacted catalytic pocket and be involved in recognizing or positioning the substrate.

DOI: 10.1007/s10930-015-9611-4
PubMed: 25957260

Affiliations:

République populaire de Chine

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Le document en format XML

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<term>Aminopeptidases (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">The proline iminopeptidase (PchPiPA) of Phanerochaete chrysosporium catalyze specifically hydrolysis of N-terminal proline from peptides. The substrate Pro-pNA was docked into the catalytic pocket and several amino acid residues were identified to interact or associate with the substrate. Eight residues were selected for site-directed mutagenesis. The wild-type and mutant proteins were expressed in Escherichia coli and purified. Kinetic parameters were calculated by hydrolyzing Pro-pNA for these enzymes. Substitution of two Glu residues (Glu198 and Glu227) which interact with the substrate via formation of hydrogen bond, led to deleterious effect on catalytic efficiency (k(cat)/K(m)) due to decrease of k(cat) and increase of K(m). Four Phe residues consisting of catalytic pocket and surrounding the docked substrate, were substituted with Ala, resulting in decrease in k(cat)/K(m) to various extents. Substitution of two residues (Val267 and Cys267) localized at the deep end of the catalytic pocket also yielded negative influence on the substrate hydrolysis. Besides, all the mutants except E227Q exhibited lower thermostability than the wild-type did, indicating that these mutations may modulate the local structure. In conclusion, these amino acid residues may play an important role in maintaining local environment of the impacted catalytic pocket and be involved in recognizing or positioning the substrate.</div>
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<Abstract><AbstractText>The proline iminopeptidase (PchPiPA) of Phanerochaete chrysosporium catalyze specifically hydrolysis of N-terminal proline from peptides. The substrate Pro-pNA was docked into the catalytic pocket and several amino acid residues were identified to interact or associate with the substrate. Eight residues were selected for site-directed mutagenesis. The wild-type and mutant proteins were expressed in Escherichia coli and purified. Kinetic parameters were calculated by hydrolyzing Pro-pNA for these enzymes. Substitution of two Glu residues (Glu198 and Glu227) which interact with the substrate via formation of hydrogen bond, led to deleterious effect on catalytic efficiency (k(cat)/K(m)) due to decrease of k(cat) and increase of K(m). Four Phe residues consisting of catalytic pocket and surrounding the docked substrate, were substituted with Ala, resulting in decrease in k(cat)/K(m) to various extents. Substitution of two residues (Val267 and Cys267) localized at the deep end of the catalytic pocket also yielded negative influence on the substrate hydrolysis. Besides, all the mutants except E227Q exhibited lower thermostability than the wild-type did, indicating that these mutations may modulate the local structure. In conclusion, these amino acid residues may play an important role in maintaining local environment of the impacted catalytic pocket and be involved in recognizing or positioning the substrate.</AbstractText>
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<ArticleIdList><ArticleId IdType="pubmed">7934933</ArticleId>
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Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.

Studies on the molecular docking and amino Acid residues involving in recognition of substrate in proline iminopeptidase by site-directed mutagenesis.

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