Purification, characterization, and gene cloning of Ceriporiopsis sp. strain MD-1 peroxidases that decolorize human hair melanin.
Identifieur interne : 000683 ( Main/Corpus ); précédent : 000682; suivant : 000684Purification, characterization, and gene cloning of Ceriporiopsis sp. strain MD-1 peroxidases that decolorize human hair melanin.
Auteurs : Kenji Nagasaki ; Masaro Kumazawa ; Shuichiro Murakami ; Shinji Takenaka ; Kenzo Koike ; Kenji AokiSource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2008.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cloning, Molecular (MeSH), Enzyme Stability (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Hair (metabolism), Hair Color (MeSH), Hemeproteins (genetics), Hemeproteins (metabolism), Humans (MeSH), Hydrogen Peroxide (metabolism), Hydrogen-Ion Concentration (MeSH), Manganese (metabolism), Melanins (metabolism), Molecular Sequence Data (MeSH), Peroxidases (analysis), Peroxidases (metabolism), Polyporales (enzymology), Polyporales (genetics), Polyporales (metabolism), Soil Microbiology (MeSH), Substrate Specificity (MeSH), Temperature (MeSH).
- MESH :
- chemical , analysis : Peroxidases.
- chemical , genetics : Fungal Proteins, Hemeproteins.
- chemical , metabolism : Fungal Proteins, Hemeproteins, Hydrogen Peroxide, Manganese, Melanins, Peroxidases.
- enzymology : Polyporales.
- genetics : Polyporales.
- metabolism : Hair, Polyporales.
- Amino Acid Sequence, Cloning, Molecular, Enzyme Stability, Hair Color, Humans, Hydrogen-Ion Concentration, Molecular Sequence Data, Soil Microbiology, Substrate Specificity, Temperature.
Abstract
Ceriporiopsis sp. strain MD-1, isolated from forest soil, produced several extracellular enzymes that decolorized human hair melanin. Among them, three enzymes (E1, E2-1, and E2-2) were purified to homogeneity and characterized. The enzymes required hydrogen peroxide in their enzyme reactions and, typical of other fungal peroxidases, oxidized various phenol compounds such as guaiacol, but not 3,4-dimethoxybenzyl alcohol. The spectra of the three enzymes showed an absorption maximum at 406 nm, indicating that they were heme proteins. However, the A(406)/A(280) values of the enzymes were below 0.4, which was lower than those of other peroxidases. E2-1 and E2-2 were similar to each other in their molecular and catalytic properties, and they possibly represent products of posttranslational modifications and/or allelic variants of the same gene, mdcA. The corresponding cDNA was cloned and sequenced; the deduced amino acid sequence showed high identities to the manganese peroxidases from other microorganisms. The specific activities and K(m) values of E2-1 and E2-2 for synthetic and human hair melanins were much higher than those of Phanerochaete chrysosporium manganese peroxidase and lignin peroxidase.
DOI: 10.1128/AEM.00253-08
PubMed: 18586974
PubMed Central: PMC2519264
Links to Exploration step
pubmed:18586974Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Purification, characterization, and gene cloning of Ceriporiopsis sp. strain MD-1 peroxidases that decolorize human hair melanin.</title><author><name sortKey="Nagasaki, Kenji" sort="Nagasaki, Kenji" uniqKey="Nagasaki K" first="Kenji" last="Nagasaki">Kenji Nagasaki</name><affiliation><nlm:affiliation>Graduate School of Agricultural Science, Kobe University, Rokko, Kobe 657-8501, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kumazawa, Masaro" sort="Kumazawa, Masaro" uniqKey="Kumazawa M" first="Masaro" last="Kumazawa">Masaro Kumazawa</name></author><author><name sortKey="Murakami, Shuichiro" sort="Murakami, Shuichiro" uniqKey="Murakami S" first="Shuichiro" last="Murakami">Shuichiro Murakami</name></author><author><name sortKey="Takenaka, Shinji" sort="Takenaka, Shinji" uniqKey="Takenaka S" first="Shinji" last="Takenaka">Shinji Takenaka</name></author><author><name sortKey="Koike, Kenzo" sort="Koike, Kenzo" uniqKey="Koike K" first="Kenzo" last="Koike">Kenzo Koike</name></author><author><name sortKey="Aoki, Kenji" sort="Aoki, Kenji" uniqKey="Aoki K" first="Kenji" last="Aoki">Kenji Aoki</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18586974</idno><idno type="pmid">18586974</idno><idno type="doi">10.1128/AEM.00253-08</idno><idno type="pmc">PMC2519264</idno><idno type="wicri:Area/Main/Corpus">000683</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000683</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Purification, characterization, and gene cloning of Ceriporiopsis sp. strain MD-1 peroxidases that decolorize human hair melanin.</title><author><name sortKey="Nagasaki, Kenji" sort="Nagasaki, Kenji" uniqKey="Nagasaki K" first="Kenji" last="Nagasaki">Kenji Nagasaki</name><affiliation><nlm:affiliation>Graduate School of Agricultural Science, Kobe University, Rokko, Kobe 657-8501, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kumazawa, Masaro" sort="Kumazawa, Masaro" uniqKey="Kumazawa M" first="Masaro" last="Kumazawa">Masaro Kumazawa</name></author><author><name sortKey="Murakami, Shuichiro" sort="Murakami, Shuichiro" uniqKey="Murakami S" first="Shuichiro" last="Murakami">Shuichiro Murakami</name></author><author><name sortKey="Takenaka, Shinji" sort="Takenaka, Shinji" uniqKey="Takenaka S" first="Shinji" last="Takenaka">Shinji Takenaka</name></author><author><name sortKey="Koike, Kenzo" sort="Koike, Kenzo" uniqKey="Koike K" first="Kenzo" last="Koike">Kenzo Koike</name></author><author><name sortKey="Aoki, Kenji" sort="Aoki, Kenji" uniqKey="Aoki K" first="Kenji" last="Aoki">Kenji Aoki</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="eISSN">1098-5336</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Hair (metabolism)</term><term>Hair Color (MeSH)</term><term>Hemeproteins (genetics)</term><term>Hemeproteins (metabolism)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Manganese (metabolism)</term><term>Melanins (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (analysis)</term><term>Peroxidases (metabolism)</term><term>Polyporales (enzymology)</term><term>Polyporales (genetics)</term><term>Polyporales (metabolism)</term><term>Soil Microbiology (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Hemeproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Hemeproteins</term><term>Hydrogen Peroxide</term><term>Manganese</term><term>Melanins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Polyporales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Polyporales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Hair</term><term>Polyporales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cloning, Molecular</term><term>Enzyme Stability</term><term>Hair Color</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Soil Microbiology</term><term>Substrate Specificity</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ceriporiopsis sp. strain MD-1, isolated from forest soil, produced several extracellular enzymes that decolorized human hair melanin. Among them, three enzymes (E1, E2-1, and E2-2) were purified to homogeneity and characterized. The enzymes required hydrogen peroxide in their enzyme reactions and, typical of other fungal peroxidases, oxidized various phenol compounds such as guaiacol, but not 3,4-dimethoxybenzyl alcohol. The spectra of the three enzymes showed an absorption maximum at 406 nm, indicating that they were heme proteins. However, the A(406)/A(280) values of the enzymes were below 0.4, which was lower than those of other peroxidases. E2-1 and E2-2 were similar to each other in their molecular and catalytic properties, and they possibly represent products of posttranslational modifications and/or allelic variants of the same gene, mdcA. The corresponding cDNA was cloned and sequenced; the deduced amino acid sequence showed high identities to the manganese peroxidases from other microorganisms. The specific activities and K(m) values of E2-1 and E2-2 for synthetic and human hair melanins were much higher than those of Phanerochaete chrysosporium manganese peroxidase and lignin peroxidase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18586974</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>74</Volume><Issue>16</Issue><PubDate><Year>2008</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Purification, characterization, and gene cloning of Ceriporiopsis sp. strain MD-1 peroxidases that decolorize human hair melanin.</ArticleTitle><Pagination><MedlinePgn>5106-12</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.00253-08</ELocationID><Abstract><AbstractText>Ceriporiopsis sp. strain MD-1, isolated from forest soil, produced several extracellular enzymes that decolorized human hair melanin. Among them, three enzymes (E1, E2-1, and E2-2) were purified to homogeneity and characterized. The enzymes required hydrogen peroxide in their enzyme reactions and, typical of other fungal peroxidases, oxidized various phenol compounds such as guaiacol, but not 3,4-dimethoxybenzyl alcohol. The spectra of the three enzymes showed an absorption maximum at 406 nm, indicating that they were heme proteins. However, the A(406)/A(280) values of the enzymes were below 0.4, which was lower than those of other peroxidases. E2-1 and E2-2 were similar to each other in their molecular and catalytic properties, and they possibly represent products of posttranslational modifications and/or allelic variants of the same gene, mdcA. The corresponding cDNA was cloned and sequenced; the deduced amino acid sequence showed high identities to the manganese peroxidases from other microorganisms. The specific activities and K(m) values of E2-1 and E2-2 for synthetic and human hair melanins were much higher than those of Phanerochaete chrysosporium manganese peroxidase and lignin peroxidase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nagasaki</LastName><ForeName>Kenji</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Graduate School of Agricultural Science, Kobe University, Rokko, Kobe 657-8501, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumazawa</LastName><ForeName>Masaro</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Murakami</LastName><ForeName>Shuichiro</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Takenaka</LastName><ForeName>Shinji</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Koike</LastName><ForeName>Kenzo</ForeName><Initials>K</Initials></Author><Author 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