Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
Author:
Publisher
Elsevier BV
Subject
Applied Microbiology and Biotechnology,Bioengineering,Biotechnology
Reference22 articles.
1. Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough;Gonzalez;Extremophiles,1998
2. Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3;Kawarabayasi;DNA Res.,1998
3. L-Threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies;Epperly;J. Biol. Chem.,1991
4. Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cystein-38;Johnson;Arch. Biochem. Biophys.,1998
5. L-Threonine dehydrogenase of chicken liver. Purification, characterization, and physiological significance;Aoyama;J. Biol. Chem.,1981
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