DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, SJ | - |
dc.contributor.author | Kim, JA | - |
dc.contributor.author | Lee, SB | - |
dc.date.accessioned | 2017-07-19T12:15:10Z | - |
dc.date.available | 2017-07-19T12:15:10Z | - |
dc.date.created | 2016-01-15 | - |
dc.date.issued | 2015-06 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/35518 | - |
dc.description.abstract | Recently, we have shown that Postechiella marina M091 degrades 3,6-anhydro-L-galactose (L-AnG) to pyruvate and D-glyceraldehyde-3-phosphate via six enzyme-catalyzed reactions and that the L-AnG dehydrogenase, an enzyme catalyzing the first step of L-AnG degradation, converts L-AnG to 3,6-anhydro-L-galactonate (L-AnGA). In this study, we report the identification and characterization of L-AnGA cycloisomerase (L-AnGACI), a novel enzyme that catalyzes the second step of L-AnG metabolism in agar-degrading microorganisms. To characterize this enzyme, the L-AnGACI gene (M091_0722) from P. marina (Pm_L-AnGACI) was cloned and expressed in E. coli. The recombinant Pm_L-AnGACI catalyzed conversion of LAnGA to 2-keto-3-deoxy-L-galactonate (L-KDGal), which was confirmed by the L-KDGal aldolase reaction and the LC-MS analysis of the aldolase reaction products. The enzyme showed activity only towards L-AnGA (100%) and galactarate (1.8%) among the 12 sugar acids and carboxylates tested, and the enzyme activity was maximal at 30A degrees C and pH 8.0. Enzyme activity was enhanced by addition of divalent ions such as Co2+ and Mg2+, as is observed from enzymes of the enolase superfamily. L-AnGACI conserves several residues commonly found in the enolase superfamily, including three metal-ion binding ligands (Asp(198), Glu(224), Glu(250)) and five active-site residues (Lys(167), Lys(169), Asp(273), His(300), Glu(320)). Phylogenetic analysis of amino acid sequences indicates that Pm_L-AnGACI belongs to a novel family within the mandelate racemase subgroup of the enolase superfamily. A reaction mechanism for cycloisomerization of L-AnGA to L-KDGal is proposed, which implies that the absolute configuration does not change during the reaction. To our knowledge, this is the first report on the characterization of L-AnGACI. | - |
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-galactonate Cycloisomerase Belonging to the Enolase Superfamily | - |
dc.type | Article | - |
dc.identifier.doi | 10.1007/S12257-015-0359-7 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.20, no.3, pp.462 - 472 | - |
dc.identifier.wosid | 000358279600012 | - |
dc.date.tcdate | 2019-03-01 | - |
dc.citation.endPage | 472 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 462 | - |
dc.citation.title | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
dc.citation.volume | 20 | - |
dc.contributor.affiliatedAuthor | Lee, SB | - |
dc.identifier.scopusid | 2-s2.0-84937856762 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 3 | - |
dc.description.scptc | 3 | * |
dc.date.scptcdate | 2018-05-121 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | MUCONATE LACTONIZING ENZYME | - |
dc.subject.keywordPlus | ENTNER-DOUDOROFF PATHWAY | - |
dc.subject.keywordPlus | THERMOPLASMA-ACIDOPHILUM | - |
dc.subject.keywordPlus | MANDELATE RACEMASE | - |
dc.subject.keywordPlus | 2-KETO-3-DEOXY-D-GLUCONATE KINASE | - |
dc.subject.keywordPlus | ALDEHYDE DEHYDROGENASE | - |
dc.subject.keywordPlus | DIVERGENT EVOLUTION | - |
dc.subject.keywordPlus | CARBOXYLIC-ACIDS | - |
dc.subject.keywordPlus | ALPHA-PROTONS | - |
dc.subject.keywordPlus | MICROORGANISMS | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactonate cycloisomerase | - |
dc.subject.keywordAuthor | enolase superfamily | - |
dc.subject.keywordAuthor | mandelate racemase | - |
dc.subject.keywordAuthor | 3,6-anhydro-L-galactose | - |
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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