Recognition Site for the Side Chain of 2-Ketoacid Substrate in D-Lactate Dehydrogenase

Replacement of Tyr52 with Val or Ala in Lactobacillus pentosus D-lactate dehydrogenase induced high activity and preference for large aliphatic 2-ketoacids and phenylpyruvate. On the other hand, replacements with Arg, Thr or Asp severely reduced the enzyme activity, and the Tyr52Arg enzyme, the only...

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Veröffentlicht in:	Journal of biochemistry (Tokyo) 2005-12, Vol.138 (6), p.741-749
Hauptverfasser:	Ishikura, Yoshirou, Tsuzuki, Shino, Takahashi, O, Tokuda, Chizuka, Nakanishi, Rie, Shinoda, Takeshi, Taguchi, Hayao
Format:	Artikel
Sprache:	eng
Schlagworte:	2-(N-morpholino)ethane sulfonic acid 2-HydDH 2-hydroxyacid dehydrogenase Amino Acid Sequence Bacterial Proteins Binding Sites d-2-hydroxyisocaproate dehydrogenase d-3-phosphoglycerate dehydrogenase d-GDH d-glycerate dehydrogenase d-HicDH d-lactate dehydrogenase d-LDH d-PGDH enzyme catalysis Keto Acids - chemistry L-Lactate Dehydrogenase - chemistry L-Lactate Dehydrogenase - metabolism Lactobacillus - enzymology Lactobacillus pentosus MES NAD SDS-PAGE sodium dodecylsulfate polyacrylamide gel electrophoresis Solvents substrate specificity
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