DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, SH | - |
dc.contributor.author | Lee, SB | - |
dc.date.accessioned | 2016-04-01T09:13:58Z | - |
dc.date.available | 2016-04-01T09:13:58Z | - |
dc.date.created | 2009-03-20 | - |
dc.date.issued | 2005-04-01 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.other | 2005-OAK-0000010540 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/29696 | - |
dc.description.abstract | The extremely thermoacidophilic archaeon Sulfolobus solfataricus utilizes D-glucose as a sole carbon and energy source through the non-phosphorylated Entner-Doudoroff pathway. It has been suggested that this micro-organism metabolizes D-gluconate, the oxidized form of D-glucose, to pyruvate and D-glyceraldehyde by using two unique enzymes, D-gluconate dehydratase and 2-keto-3-deoxy-D-gluconate aldolase. In the present study, we report the purification and characterization of D-gluconate dehydratase from S. solfataricus, which catalyses the conversion of D-gluconate into 2-keto-3-deoxy-D-gluconate. D-Gluconate dehydratase was purified 400-fold from extracts of S. solfataricus by ammonium sulphate fractionation and chromatography on DEAE-Sepharose, Q-Sepharose, phenyl-Sepharose and Mono Q. The native protein showed a molecular mass of 350 kDa by gel filtration, whereas SDS/PAGE analysis provided a molecular mass of 44 kDa, indicating that D-gluconate dehydratase is an octameric protein. The enzyme showed maximal activity at temperatures between 80 and 90 degrees C and pH values between 6.5 and 7.5, and a half-life of 40 min at 100 degrees C. Bivalent metal ions such as Co2+, Mg2+, Mn2+ and Ni2+ activated, whereas EDTA inhibited the enzyme. A metal analysis of the purified protein revealed the presence of one Co2+ ion per enzyme monomer. Of the 22 aldonic acids tested, only D-gluconate served as a substrate, with K-m = 0.45 mM and V-max = 0.15 unit/mg of enzyme. From N-terminal sequences of the purified enzyme, it was found that the gene product of SSO3198 in the S. solfataricus genome database corresponded to D-gluconate dehydratase (gnaD). We also found that the D-gluconate dehydratase of S. solfataricus is a phosphoprotein and that its catalytic activity is regulated by a phosphorylation-dephosphorylation mechanism. This is the first report on biochemical and genetic characterization of D-gluconate dehydratase involved in the non-phosphorylated Entner-Doudoroff pathway. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | PORTLAND PRESS LTD | - |
dc.relation.isPartOf | BIOCHEMICAL JOURNAL | - |
dc.subject | gluconate dehydratase | - |
dc.subject | metalloprotein | - |
dc.subject | non-phosphorylated Entner-Doudoroff pathway | - |
dc.subject | phosphoprotein | - |
dc.subject | Sulfolobus solftaricus | - |
dc.subject | thermoacidophilic archaeon | - |
dc.subject | HYPERTHERMOPHILIC ARCHAEON-SULFOLOBUS | - |
dc.subject | ARCHAEBACTERIUM SULFOLOBUS | - |
dc.subject | THERMOPLASMA-ACIDOPHILUM | - |
dc.subject | CLOSTRIDIUM-PASTEURIANUM | - |
dc.subject | PHOSPHORYLATION SITES | - |
dc.subject | MOLECULAR-BIOLOGY | - |
dc.subject | CARBOXYLIC-ACIDS | - |
dc.subject | PROTEIN-KINASES | - |
dc.subject | ALPHA-PROTONS | - |
dc.subject | TRANSCRIPTION | - |
dc.title | Identification and characterization of Sulfolobus solfataricus D-gluconate dehydratase: a key enzyme in the non-phosphorylated Entner-Doudoroff pathway | - |
dc.type | Article | - |
dc.contributor.college | 경북씨그랜트센터 | - |
dc.identifier.doi | 10.1042/BJ20041053 | - |
dc.author.google | Kim, SH | - |
dc.author.google | Lee, SB | - |
dc.relation.volume | 387 | - |
dc.relation.startpage | 271 | - |
dc.relation.lastpage | 280 | - |
dc.contributor.id | 10105619 | - |
dc.relation.journal | BIOCHEMICAL JOURNAL | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL JOURNAL, v.387, pp.271 - 280 | - |
dc.identifier.wosid | 000228431900029 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 280 | - |
dc.citation.startPage | 271 | - |
dc.citation.title | BIOCHEMICAL JOURNAL | - |
dc.citation.volume | 387 | - |
dc.contributor.affiliatedAuthor | Lee, SB | - |
dc.identifier.scopusid | 2-s2.0-17144427281 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 48 | - |
dc.description.scptc | 50 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | HYPERTHERMOPHILIC ARCHAEON-SULFOLOBUS | - |
dc.subject.keywordPlus | ARCHAEBACTERIUM SULFOLOBUS | - |
dc.subject.keywordPlus | THERMOPLASMA-ACIDOPHILUM | - |
dc.subject.keywordPlus | CLOSTRIDIUM-PASTEURIANUM | - |
dc.subject.keywordPlus | PHOSPHORYLATION SITES | - |
dc.subject.keywordPlus | MOLECULAR-BIOLOGY | - |
dc.subject.keywordPlus | CARBOXYLIC-ACIDS | - |
dc.subject.keywordPlus | PROTEIN-KINASES | - |
dc.subject.keywordPlus | ALPHA-PROTONS | - |
dc.subject.keywordPlus | TRANSCRIPTION | - |
dc.subject.keywordAuthor | gluconate dehydratase | - |
dc.subject.keywordAuthor | metalloprotein | - |
dc.subject.keywordAuthor | non-phosphorylated Entner-Doudoroff pathway | - |
dc.subject.keywordAuthor | phosphoprotein | - |
dc.subject.keywordAuthor | Sulfolobus solftaricus | - |
dc.subject.keywordAuthor | thermoacidophilic archaeon | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
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