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Substrate Diversity of L-Threonic Acid Dehydrogenase Homologs

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Abstract

Despite physiological importance of aldonic sugar acids for living organisms, little is known about metabolic pathways of these compounds. Here, we investigated the functional diversity of homologs of L-threonic acid dehydrogenase (ThrDH; UniProt ID: Q0KBC7), an enzyme composed of two NAD-binding domains (PF14833 and PF03446). Ten ThrDH homologs with different genomic context were studied; seven new enzymatic activities were identified, such as (R)-pantoate dehydrogenase, L-altronic acid dehydrogenase, 6-deoxy-L-talonate dehydrogenase, L-idonic acid dehydrogenase, D-xylonic acid dehydrogenase, D-gluconic acid dehydrogenase, and 2-hydroxy-3-oxopantoate reductase activities. Two associated metabolic pathways were identified: L-idonic acid dehydrogenase was found to be involved in the degradation of L-idonic acid through oxidation/decarboxylation in Agrobacterium radiobacter K84, while 2-hydroxy-3-oxopantoate reductase was found to participate in D-glucarate catabolism through dehydration/cleavage in Ralstonia metallidurans CH34.

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Abbreviations

EryDH:

D-erythronic acid dehydrogenase

PanDH:

(R)-pantoate dehydrogenase

SSN:

sequence similarity network

ThrDH:

L-threonic acid dehydrogenase

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Funding

This work was supported by the National Natural Science Foundation of China (project No. 31970087) and the start-up grant from the South China Normal University.

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Authors and Affiliations

  1. Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Sciences, South China Normal University, 510631, Guangzhou, Guangdong, China

    C. F. Zhang, Y. P. Liu, X. X. Wu & H. Huang

  2. Institute of Ecological Science, School of Life Sciences, South China Normal University, 510631, Guangzhou, Guangdong, China

    X. S. Zhang

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  1. C. F. Zhang
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  2. Y. P. Liu
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  3. X. X. Wu
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  4. X. S. Zhang
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  5. H. Huang
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Correspondence to X. S. Zhang or H. Huang.

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This article does not contain description of studies with human participants or animals performed by any of the authors. The authors declare no conflict of interest.

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Zhang, C., Liu, Y., Wu, X. et al. Substrate Diversity of L-Threonic Acid Dehydrogenase Homologs. Biochemistry Moscow 85, 463–471 (2020). https://doi.org/10.1134/S0006297920040069

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  • DOI: https://doi.org/10.1134/S0006297920040069

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