Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii
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- Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii
- Kim, Sangwoo; Gu, Sol-A; Kim, Yong Hwan; Kim, Kyung-Jin
- D-Lactate dehydrogenase; Lactobacillus jensenii; Polylactic acid
- Issue Date
- ELSEVIER SCIENCE BV
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.68, no., pp.151 - 157
- 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.
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