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Title: Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity

Source: Protein Science. 29(12): 2387-2397.

Author(s)Chauliac, Diane ; Wang, Qingzhao ; St. John, Franz J.; Jones, Grace ; Hurlbert, Jason C.; Ingram, Lonnie O.; Shanmugam, Keelnatham T.

Publication Year: 2020  View PDF »

Category: Journal Articles

Abstract: During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a D-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 γ-O and the C1 carboxylate of pyruvate. To our knowledge, this is the first GDH to gain LDH activity due to an active site amino acid change, a desired result of in vivo enzyme evolution.

Keywords: Bacillus coagulans; directed evolution; D-lactic acid; glycerol dehydrogenase; lactate dehydrogenase

Publication Review Process: Formally Refereed

File size: 2,048 kb(s)

Date posted: 01/06/2021

This publication is also viewable on Treesearch:  view
RITS Product ID: 10086
Current FPL Scientist associated with this product
St. Johns, Franz
Research Microbiologist

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