DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, SJ | - |
dc.contributor.author | Lee, SB | - |
dc.date.accessioned | 2016-03-31T07:23:00Z | - |
dc.date.available | 2016-03-31T07:23:00Z | - |
dc.date.created | 2015-02-27 | - |
dc.date.issued | 2014-11 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.other | 2014-OAK-0000032379 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/13572 | - |
dc.description.abstract | The complete hydrolysis of agarose produces its monomeric sugars, D-galactose and 3,6-anhydro-Lgalactose (L-AnG). Although enzymes of D-galactose metabolism are well characterized, those involved in L-AnG metabolism have not yet been investigated. In this study, we report the identification and characterization of L-AnG dehydrogenase (L-AnGDH), an aldehyde dehydrogenase (ALDH), catalyzing the first step of L-AnG degradation. To compare substrate and cofactor specificities of L-AnGDH, two L-AnGDH genes obtained from the marine bacterium Postechiella marina (Pm_L-AnGDH) and the soil bacterium Streptomyces coelicolor (Sc_L-AnGDH) were cloned and expressed in E. coli. Whereas the recombinant Pm_LAnGDH and Sc_L-AnGDH were similar in their oligomeric state (homotetramer) and optimum reaction conditions (30a"integral, pH 8.0), the two enzymes were distinguishable by their substrate and cofactor specificities. Sc_L-AnGDH catalyzed the oxidation of L-AnG using both NAD(+) and NADP(+), with a preference for NAD(+). It also catalyzed the dehydrogenation of L-glyceraldehyde, glycolaldehyde, and L-lactaldehyde in the presence of NAD(+). On the other hand, Pm_L-AnGDH showed exclusive selectivity towards NADP(+) and did not oxidize aldehydes other than L-AnG and L-glyceraldehyde. The phylogenetic analysis of amino sequences indicated that L-AnGDH belongs to a novel subfamily within the ALDH superfamily. To our knowledge, this is the first report on the characterization of L-AnGDH. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
dc.relation.isPartOf | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.title | Identification and characterization of 3,6-anhydro-L-galactose dehydrogenases belonging to the aldehyde dehydrogenase superfamily from marine and soil microorganisms | - |
dc.type | Article | - |
dc.contributor.college | 엔지니어링 대학원 | - |
dc.identifier.doi | 10.1007/S12257-014-0830-X | - |
dc.author.google | Cho, SJ | - |
dc.author.google | Lee, SB | - |
dc.relation.volume | 19 | - |
dc.relation.issue | 6 | - |
dc.relation.startpage | 1058 | - |
dc.relation.lastpage | 1068 | - |
dc.contributor.id | 10105619 | - |
dc.relation.journal | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCIE | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.19, no.6, pp.1058 - 1068 | - |
dc.identifier.wosid | 000348046500016 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 1068 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 1058 | - |
dc.citation.title | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.citation.volume | 19 | - |
dc.contributor.affiliatedAuthor | Lee, SB | - |
dc.identifier.scopusid | 2-s2.0-84921019100 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 5 | - |
dc.description.scptc | 4 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | LACTALDEHYDE DEHYDROGENASE | - |
dc.subject.keywordPlus | METABOLIC PATHWAYS | - |
dc.subject.keywordPlus | XYLOSE REDUCTASE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | HYDROLYSIS | - |
dc.subject.keywordPlus | AGAR | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | PREFERENCE | - |
dc.subject.keywordPlus | CONVERSION | - |
dc.subject.keywordPlus | HYDROLASE | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactose dehydrogenase | - |
dc.subject.keywordAuthor | aldehyde dehydrogenase superfamily | - |
dc.subject.keywordAuthor | cofactor specificity | - |
dc.subject.keywordAuthor | agarose metabolism | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
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