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L-aspartate dehydrogenase: features and applications.
Yinxia Li1, Henry Joseph Oduor Ogola, Yoshihiro Sawa
1Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue, Shimane, 690-8504, Japan.
Applied Microbiology and Biotechnology
|November 29, 2011
Summary
L-aspartate dehydrogenase (L-AspDH) is a newly discovered enzyme superfamily member with potential industrial applications. Research highlights its unique classification and promising catalytic properties for biocatalysis at room temperature.
Area of Science:
- Biochemistry and enzymology
- Biotechnology and industrial biocatalysis
Background:
- L-amino acid dehydrogenases catalyze reversible oxidative deamination of L-amino acids to 2-oxoacids using NAD(+) or NADP(+) cofactors.
- These enzymes have broad applications in synthesizing amino acids, developing biosensors, and regenerating coenzymes for industrial processes.
Purpose of the Study:
- To review available data on the L-aspartate dehydrogenase (L-AspDH) superfamily member.
- To discuss its catalytic properties, physiological roles, and biotechnological potential.
Main Methods:
- Bioinformatic analysis for enzyme classification.
- Review of existing enzymological and biochemical data.
Main Results:
- L-AspDH is proposed to be classified into NadB (NAD biosynthesis-related) and non-NadB types based on bioinformatic and in vivo data.
- Mesophilic non-NadB type L-AspDH exhibits promising catalytic properties at room temperature, indicating potential as industrial biocatalysts.
Conclusions:
- L-AspDH represents a novel group of amino acid dehydrogenases with significant biotechnological promise.
- Further identification and extensive enzymological research on new L-AspDH members are crucial to fully understand their functions and applications.
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