Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'1.
Identifieur interne : 000192 ( Main/Exploration ); précédent : 000191; suivant : 000193Activity 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
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Rosa</name><affiliation wicri:level="4"><nlm:affiliation>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP</wicri:regionArea><placeName><region type="state">État de São Paulo</region><settlement type="city">São Paulo</settlement></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author><author><name sortKey="Cabral, Hamilton" sort="Cabral, Hamilton" uniqKey="Cabral H" first="Hamilton" last="Cabral">Hamilton Cabral</name><affiliation wicri:level="4"><nlm:affiliation>Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brazil. Electronic address: hamilton@fcfrp.usp.br.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo</wicri:regionArea><placeName><settlement type="city">São Paulo</settlement><region type="state">État de São Paulo</region></placeName><orgName type="university">Université de São Paulo</orgName></affiliation></author></analytic><series><title level="j">International journal of biological macromolecules</title><idno type="eISSN">1879-0003</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><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><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><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></keywords></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27771408</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>09</Day></DateCompleted><DateRevised><Year>2017</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0003</ISSN><JournalIssue CitedMedium="Internet"><Volume>94</Volume><Issue>Pt A</Issue><PubDate><Year>2017</Year><Month>Jan</Month></PubDate></JournalIssue><Title>International journal of biological macromolecules</Title><ISOAbbreviation>Int J Biol Macromol</ISOAbbreviation></Journal><ArticleTitle>Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'<sub>1</sub>.</ArticleTitle><Pagination><MedlinePgn>474-483</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-8130(16)31050-9</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijbiomac.2016.10.063</ELocationID><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></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Oliveira</LastName><ForeName>Lilian Caroline Gonçalves</ForeName><Initials>LCG</Initials><AffiliationInfo><Affiliation>Universidade Federal de São Paulo, UNIFESP, São Paulo, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Juliano</LastName><ForeName>Maria Aparecida</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Universidade Federal de São Paulo, UNIFESP, São Paulo, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Juliano</LastName><ForeName>Luiz</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Universidade Federal de São Paulo, UNIFESP, São Paulo, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rosa</LastName><ForeName>Jose C</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cabral</LastName><ForeName>Hamilton</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brazil. Electronic address: hamilton@fcfrp.usp.br.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>10</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biol Macromol</MedlineTA><NlmUniqueID>7909578</NlmUniqueID><ISSNLinking>0141-8130</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015853">Cysteine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D057056">Cysteine Proteases</NameOfSubstance></Chemical><Chemical><RegistryNumber>K3Z4F929H6</RegistryNumber><NameOfSubstance UI="D008239">Lysine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055162" MajorTopicYN="N">Biocatalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057056" MajorTopicYN="N">Cysteine Proteases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015853" MajorTopicYN="N">Cysteine Proteinase Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008239" MajorTopicYN="N">Lysine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059748" MajorTopicYN="N">Proteolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cysteine protease</Keyword><Keyword MajorTopicYN="Y">Fungal protease</Keyword><Keyword MajorTopicYN="Y">High specificity</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>07</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>10</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>10</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>5</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27771408</ArticleId><ArticleId IdType="pii">S0141-8130(16)31050-9</ArticleId><ArticleId IdType="doi">10.1016/j.ijbiomac.2016.10.063</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Brésil</li></country><region><li>État de São Paulo</li></region><settlement><li>São Paulo</li></settlement><orgName><li>Université de São Paulo</li></orgName></list><tree><country name="Brésil"><region name="État de São Paulo"><name sortKey="Da Silva, Ronivaldo Rodrigues" sort="Da Silva, Ronivaldo Rodrigues" uniqKey="Da Silva R" first="Ronivaldo Rodrigues" last="Da Silva">Ronivaldo Rodrigues Da Silva</name></region><name sortKey="Cabral, Hamilton" sort="Cabral, Hamilton" uniqKey="Cabral H" first="Hamilton" last="Cabral">Hamilton Cabral</name><name sortKey="De Oliveira, Lilian Caroline Goncalves" sort="De Oliveira, Lilian Caroline Goncalves" uniqKey="De Oliveira L" first="Lilian Caroline Gonçalves" last="De Oliveira">Lilian Caroline Gonçalves De Oliveira</name><name sortKey="Juliano, Luiz" sort="Juliano, Luiz" uniqKey="Juliano L" first="Luiz" last="Juliano">Luiz Juliano</name><name sortKey="Juliano, Maria Aparecida" sort="Juliano, Maria Aparecida" uniqKey="Juliano M" first="Maria Aparecida" last="Juliano">Maria Aparecida Juliano</name><name sortKey="Rosa, Jose C" sort="Rosa, Jose C" uniqKey="Rosa J" first="Jose C" last="Rosa">Jose C. 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