Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity
Abstract
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.
- Authors:
-
[3];
- Department of Microbiology and Cell Science University of Florida Gainesville Florida USA, Galactic Brussels Belgium
- Department of Microbiology and Cell Science University of Florida Gainesville Florida USA, BP Bioscience Center San Diego California USA
- Forest Products Laboratory USDA Forest Service Madison Wisconsin USA
- Department of Chemistry, Physics and Geology Winthrop University Rock Hill South Carolina USA
- Department of Microbiology and Cell Science University of Florida Gainesville Florida USA
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1804779
- Grant/Contract Number:
- DE‐PI0000031; W‐31‐109‐Eng‐38
- Resource Type:
- Publisher's Accepted Manuscript
- Journal Name:
- Protein Science
- Additional Journal Information:
- Journal Name: Protein Science Journal Volume: 29 Journal Issue: 12; Journal ID: ISSN 0961-8368
- Publisher:
- Wiley Blackwell (John Wiley & Sons)
- Country of Publication:
- United Kingdom
- Language:
- English
Citation Formats
Chauliac, Diane, Wang, Qingzhao, St. John, Franz J., Jones, Grace, Hurlbert, Jason C., Ingram, Lonnie O., and Shanmugam, Keelnatham T. Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity. United Kingdom: N. p., 2020.
Web. doi:10.1002/pro.3963.
Chauliac, Diane, Wang, Qingzhao, St. John, Franz J., Jones, Grace, Hurlbert, Jason C., Ingram, Lonnie O., & Shanmugam, Keelnatham T. Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity. United Kingdom. https://doi.org/10.1002/pro.3963
Chauliac, Diane, Wang, Qingzhao, St. John, Franz J., Jones, Grace, Hurlbert, Jason C., Ingram, Lonnie O., and Shanmugam, Keelnatham T. Sat .
"Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity". United Kingdom. https://doi.org/10.1002/pro.3963.
@article{osti_1804779,
title = {Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d ‐lactate dehydrogenase activity},
author = {Chauliac, Diane and Wang, Qingzhao and St. John, Franz J. and Jones, Grace and Hurlbert, Jason C. and Ingram, Lonnie O. and Shanmugam, Keelnatham T.},
abstractNote = {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.},
doi = {10.1002/pro.3963},
journal = {Protein Science},
number = 12,
volume = 29,
place = {United Kingdom},
year = {Sat Oct 24 00:00:00 EDT 2020},
month = {Sat Oct 24 00:00:00 EDT 2020}
}
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