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DC Field | Value | Language |
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dc.citation.endPage | 157 | - |
dc.citation.startPage | 151 | - |
dc.citation.title | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | - |
dc.citation.volume | 68 | - |
dc.contributor.author | Kim, Sangwoo | - |
dc.contributor.author | Gu, Sol-A | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.contributor.author | Kim, Kyung-Jin | - |
dc.date.accessioned | 2023-12-22T02:37:17Z | - |
dc.date.available | 2023-12-22T02:37:17Z | - |
dc.date.created | 2014-05-27 | - |
dc.date.issued | 2014-07 | - |
dc.description.abstract | The thermostable d-lactate dehydrogenase from Lactobacillus jensenii (Ljd-LDH) is a key enzyme in the production of the d-form of lactic acid from pyruvate concomitant with the oxidation of NADH to NAD+. The polymers of d-lactic acid are used as biodegradable bioplastics. The crystal structures of Ljd-LDH and in complex with NAD+ were determined at 2.13 and 2.60Å resolutions, respectively. The Ljd-LDH monomer consists of the N-terminal substrate-binding domain and the C-terminal NAD-binding domain. The Ljd-LDH forms a homodimeric structure, and the C-terminal NAD-binding domain mostly enables the dimerization of the enzyme. The NAD cofactor is bound to the GxGxxG NAD-binding motif located between the two domains. Structural comparisons of Ljd-LDH with other d-LDHs reveal that Ljd-LDH has unique amino acid residues at the linker region, which indicates that the open-close dynamics of Ljd-LDH might be different from that of other d-LDHs. Moreover, thermostability experiments showed that the T5010 value of Ljd-LDH (54.5°C) was much higher than the commercially available d-lactate dehydrogenase (42.7°C). In addition, Ljd-LDH has at least a 7°C higher denaturation temperature compared to commercially available d-LDHs. | - |
dc.identifier.bibliographicCitation | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.68, pp.151 - 157 | - |
dc.identifier.doi | 10.1016/j.ijbiomac.2014.04.048 | - |
dc.identifier.issn | 0141-8130 | - |
dc.identifier.scopusid | 2-s2.0-84899904875 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/4782 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84899904875 | - |
dc.identifier.wosid | 000338414600025 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Chemistry, Applied; Polymer Science | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Chemistry; Polymer Science | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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