Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'1.
Identifieur interne : 000188 ( Main/Curation ); précédent : 000187; suivant : 000189Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'1.
Auteurs : Ronivaldo Rodrigues Da Silva [Brésil] ; Lilian Caroline Gonçalves De Oliveira [Brésil] ; Maria Aparecida Juliano [Brésil] ; Luiz Juliano [Brésil] ; Jose C. Rosa [Brésil] ; Hamilton Cabral [Brésil]Source :
- International journal of biological macromolecules [ 1879-0003 ] ; 2017.
Descripteurs français
- KwdFr :
- Biocatalyse (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Cysteine proteases (composition chimique), Cysteine proteases (isolement et purification), Inhibiteurs de la cystéine protéinase (composition chimique), Lysine (composition chimique), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Protéines fongiques (isolement et purification), Protéolyse (MeSH), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Cysteine proteases, Inhibiteurs de la cystéine protéinase, Lysine, Protéines fongiques.
- enzymologie : Phanerochaete.
- isolement et purification : Cysteine proteases, Protéines fongiques.
- Biocatalyse, Cinétique, Concentration en ions d'hydrogène, Protéolyse, Spécificité du substrat, Stabilité enzymatique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biocatalysis (MeSH), Cysteine Proteases (chemistry), Cysteine Proteases (isolation & purification), Cysteine Proteinase Inhibitors (chemistry), Enzyme Stability (MeSH), Fungal Proteins (chemistry), Fungal Proteins (isolation & purification), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Lysine (chemistry), Phanerochaete (enzymology), Proteolysis (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Cysteine Proteases, Cysteine Proteinase Inhibitors, Fungal Proteins, Lysine.
- chemical , isolation & purification : Cysteine Proteases, Fungal Proteins.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Biocatalysis, Enzyme Stability, Hydrogen-Ion Concentration, Kinetics, Proteolysis, Substrate Specificity.
Abstract
Peptidases are enzymes that catalyze the rupture of peptide bonds. Catalytic specificity studies of these enzymes have illuminated their modes of action and preferred hydrolysis targets. We describe the biochemical characteristics and catalytic specificity of a lysine-dependent peptidase secreted by the basidiomycete fungus Phanerochaete chrysosporium. We attained 5.7-fold purification of a ∼23-kDa neutral peptidase using size-exclusion (Sephadex G-50 resin) and ion-exchange (Source 15S resin) chromatography. Using the Fluorescence Resonance Energy Transfer substrate Abz-KLRSSKQ-EDDnp, we detected maximal activity at pH 7.0 and 45-55°C. The peptidase retained ∼80% of its enzymatic activity for a wide range of conditions (pH 4-9; temperatures up to 50°C for 1h). The peptidase activity was lowered by the ionic surfactants, sodium dodecyl sulfate and cetyltrimethylammonium bromide; the reducing agent, dithiothreitol; the chaotrope, guanidine; copper (II) ion; and the cysteine peptidase-specific inhibitors, iodoacetic acid and N-ethylmaleimide. The peptidase preferred the basic amino acids K and R and high selectivity on S'1 subsite, exhibiting a condition of lysine-dependence to catalysis on anchoring of this subsite.
DOI: 10.1016/j.ijbiomac.2016.10.063
PubMed: 27771408
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- to stream Main, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000188
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pubmed:27771408Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Biocatalysis (MeSH)</term>
<term>Cysteine Proteases (chemistry)</term>
<term>Cysteine Proteases (isolation & purification)</term>
<term>Cysteine Proteinase Inhibitors (chemistry)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (isolation & purification)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Lysine (chemistry)</term>
<term>Phanerochaete (enzymology)</term>
<term>Proteolysis (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Biocatalyse (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Cysteine proteases (composition chimique)</term>
<term>Cysteine proteases (isolement et purification)</term>
<term>Inhibiteurs de la cystéine protéinase (composition chimique)</term>
<term>Lysine (composition chimique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (isolement et purification)</term>
<term>Protéolyse (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Stabilité enzymatique (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Proteases</term>
<term>Cysteine Proteinase Inhibitors</term>
<term>Fungal Proteins</term>
<term>Lysine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Cysteine Proteases</term>
<term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cysteine proteases</term>
<term>Inhibiteurs de la cystéine protéinase</term>
<term>Lysine</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Cysteine proteases</term>
<term>Protéines fongiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Biocatalysis</term>
<term>Enzyme Stability</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Proteolysis</term>
<term>Substrate Specificity</term>
</keywords>
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<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Protéolyse</term>
<term>Spécificité du substrat</term>
<term>Stabilité enzymatique</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Peptidases are enzymes that catalyze the rupture of peptide bonds. Catalytic specificity studies of these enzymes have illuminated their modes of action and preferred hydrolysis targets. We describe the biochemical characteristics and catalytic specificity of a lysine-dependent peptidase secreted by the basidiomycete fungus Phanerochaete chrysosporium. We attained 5.7-fold purification of a ∼23-kDa neutral peptidase using size-exclusion (Sephadex G-50 resin) and ion-exchange (Source 15S resin) chromatography. Using the Fluorescence Resonance Energy Transfer substrate Abz-KLRSSKQ-EDDnp, we detected maximal activity at pH 7.0 and 45-55°C. The peptidase retained ∼80% of its enzymatic activity for a wide range of conditions (pH 4-9; temperatures up to 50°C for 1h). The peptidase activity was lowered by the ionic surfactants, sodium dodecyl sulfate and cetyltrimethylammonium bromide; the reducing agent, dithiothreitol; the chaotrope, guanidine; copper (II) ion; and the cysteine peptidase-specific inhibitors, iodoacetic acid and N-ethylmaleimide. The peptidase preferred the basic amino acids K and R and high selectivity on S'<sub>1</sub>
subsite, exhibiting a condition of lysine-dependence to catalysis on anchoring of this subsite.</div>
</front>
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<Title>International journal of biological macromolecules</Title>
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<ArticleTitle>Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'<sub>1</sub>
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<Abstract><AbstractText>Peptidases are enzymes that catalyze the rupture of peptide bonds. Catalytic specificity studies of these enzymes have illuminated their modes of action and preferred hydrolysis targets. We describe the biochemical characteristics and catalytic specificity of a lysine-dependent peptidase secreted by the basidiomycete fungus Phanerochaete chrysosporium. We attained 5.7-fold purification of a ∼23-kDa neutral peptidase using size-exclusion (Sephadex G-50 resin) and ion-exchange (Source 15S resin) chromatography. Using the Fluorescence Resonance Energy Transfer substrate Abz-KLRSSKQ-EDDnp, we detected maximal activity at pH 7.0 and 45-55°C. The peptidase retained ∼80% of its enzymatic activity for a wide range of conditions (pH 4-9; temperatures up to 50°C for 1h). The peptidase activity was lowered by the ionic surfactants, sodium dodecyl sulfate and cetyltrimethylammonium bromide; the reducing agent, dithiothreitol; the chaotrope, guanidine; copper (II) ion; and the cysteine peptidase-specific inhibitors, iodoacetic acid and N-ethylmaleimide. The peptidase preferred the basic amino acids K and R and high selectivity on S'<sub>1</sub>
subsite, exhibiting a condition of lysine-dependence to catalysis on anchoring of this subsite.</AbstractText>
<CopyrightInformation>Copyright © 2016 Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>da Silva</LastName>
<ForeName>Ronivaldo Rodrigues</ForeName>
<Initials>RR</Initials>
<AffiliationInfo><Affiliation>Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brazil.</Affiliation>
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<Author ValidYN="Y"><LastName>de Oliveira</LastName>
<ForeName>Lilian Caroline Gonçalves</ForeName>
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<Author ValidYN="Y"><LastName>Juliano</LastName>
<ForeName>Maria Aparecida</ForeName>
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<AffiliationInfo><Affiliation>Universidade Federal de São Paulo, UNIFESP, São Paulo, Brazil.</Affiliation>
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<Author ValidYN="Y"><LastName>Juliano</LastName>
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<AffiliationInfo><Affiliation>Universidade Federal de São Paulo, UNIFESP, São Paulo, Brazil.</Affiliation>
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<AffiliationInfo><Affiliation>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.</Affiliation>
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<Initials>H</Initials>
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