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  • Conversion of Lactobacillus pentosus D-lactate dehydrogenase to a D-hydroxyisocaproate dehydrogenase through a single amino acid replacement.

Conversion of Lactobacillus pentosus D-lactate dehydrogenase to a D-hydroxyisocaproate dehydrogenase through a single amino acid replacement.

Journal of bacteriology (2003-08-05)
Chizuka Tokuda, Yoshiro Ishikura, Mayu Shigematsu, Hiroyuki Mutoh, Shino Tsuzuki, Yusaku Nakahira, Yusuke Tamura, Takeshi Shinoda, Kazuhito Arai, O Takahashi, Hayao Taguchi
RESUMO

The single amino acid replacement of Tyr52 with Leu drastically increased the activity of Lactobacillus pentosus NAD-dependent D-lactate dehydrogenase toward larger aliphatic or aromatic 2-ketoacid substrates by 3 or 4 orders of magnitude and decreased the activity toward pyruvate by about 30-fold, converting the enzyme into a highly active D-2-hydroxyisocaproate dehydrogenase.

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Sigma-Aldrich
4-Methylvaleric acid, 99%
Sigma-Aldrich
4-Methylpentanoic acid, ≥98%, FCC, FG