Rational identification of a high catalytic efficiency leucine dehydrogenase and process development for efficient synthesis of l‐phenylglycine
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DOI: 10.1002/biot.202200465
Abstract: Enzymatic asymmetric synthesis of chiral amino acids has great industrial potential. However, the low catalytic efficiency of high‐concentration substrates limits their industrial application. Herein, using a combination of substrate catalytic efficiency prediction based on “open… read more here.
Keywords: catalytic efficiency; process development; substrate; leucine dehydrogenase ... See more keywords
Structural insights into thermostabilization of leucine dehydrogenase from its atomic structure by cryo-electron microscopy.
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DOI: 10.1016/j.jsb.2018.12.001
Abstract: Leucine dehydrogenase (LDH, EC 1.4.1.9) is a NAD+-dependent oxidoreductase that catalyzes the deamination of branched-chain l-amino acids (BCAAs). LDH of Geobacillus stearothermophilus (GstLDH) is a highly thermostable enzyme that has been applied for the quantification… read more here.
Keywords: cryo electron; microscopy; leucine dehydrogenase; electron microscopy ... See more keywords
The Crystal Structure of L-Leucine Dehydrogenase from Pseudomonas aeruginosa
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DOI: 10.14348/molcells.2022.0012
Abstract: Leucine dehydrogenase (LDH, EC 1.4.1.9) catalyzes the reversible deamination of branched-chain L-amino acids to their corresponding keto acids using NAD+ as a cofactor. LDH generally adopts an octameric structure with D4 symmetry, generating a molecular… read more here.
Keywords: structure; pseudomonas aeruginosa; leucine dehydrogenase; ldh ... See more keywords