Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'1.
Identifieur interne : 000188 ( Main/Corpus ); précédent : 000187; suivant : 000189Activity of a peptidase secreted by Phanerochaete chrysosporium depends on lysine to subsite S'1.
Auteurs : Ronivaldo Rodrigues Da Silva ; Lilian Caroline Gonçalves De Oliveira ; Maria Aparecida Juliano ; Luiz Juliano ; Jose C. Rosa ; Hamilton CabralSource :
- International journal of biological macromolecules [ 1879-0003 ] ; 2017.
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
Links to Exploration step
pubmed:27771408Le document en format XML
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Rosa</name><affiliation><nlm:affiliation>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cabral, Hamilton" sort="Cabral, Hamilton" uniqKey="Cabral H" first="Hamilton" last="Cabral">Hamilton Cabral</name><affiliation><nlm:affiliation>Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo, Brazil. 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Rosa</name><affiliation><nlm:affiliation>Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Cabral, Hamilton" sort="Cabral, Hamilton" uniqKey="Cabral H" first="Hamilton" last="Cabral">Hamilton Cabral</name><affiliation><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></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="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="enzymology" xml:lang="en"><term>Phanerochaete</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></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></record>Pour manipuler ce document sous Unix (Dilib)
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