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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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