Diversity of microbial threonine aldolases and their application

Threonine aldolase catalyzes the reversible interconversion of certain β-hydroxy-α-amino acids and glycine plus the corresponding aldehydes. Various microbial threonine aldolases with different stereospecificities were found on extensive screening, and the genes encoding the proteins were cloned and...

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Bibliographic Details
Published in:Journal of Molecular Catalysis. B, Enzymatic Enzymatic, 2000-10, Vol.10 (1), p.107-115
Main Authors: Liu, Ji-Quan, Dairi, Tohru, Itoh, Nobuya, Kataoka, Michihiko, Shimizu, Sakayu, Yamada, Hideaki
Format: Article
Language:English
Subjects:
Aldehydes
Amino acids
Biosynthesis
Catalysis
Cloning
Enzymatic resolution
Escherichia coli
Stereochemistry
Stereoselective synthesis
Threonine aldolase
β-Hydroxy-α-amino acid
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Summary:Threonine aldolase catalyzes the reversible interconversion of certain β-hydroxy-α-amino acids and glycine plus the corresponding aldehydes. Various microbial threonine aldolases with different stereospecificities were found on extensive screening, and the genes encoding the proteins were cloned and heterogeneously overexpressed in Escherichia coli. By using recombinant threonine aldolases, an enzymatic resolution process was established for the production of optically pure β-hydroxy-α-amino acids. In addition, the threonine aldolase-catalyzed direct synthesis of β-hydroxy-α-amino acid from aldehyde and glycine is discussed.
ISSN:1381-1177
1873-3158
DOI:10.1016/S1381-1177(00)00118-1