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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
1.1.1.286
660907
Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase
Biochem. Biophys. Res. Commun.
331
341-346
2005
Pyrococcus horikoshii
15845397
1.1.1.286
656127
Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase
J. Biol. Chem.
278
1864-1871
2003
Thermus thermophilus
12427751
1.1.1.286
656127
Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase
J. Biol. Chem.
278
1864-1871
2003
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
12427751
1.1.1.286
738195
Characterization of two ?-decarboxylating dehydrogenases from Sulfolobus acidocaldarius
Extremophiles
20
843-853
2016
Sulfolobus acidocaldarius
27590116
1.1.1.286
738195
Characterization of two ?-decarboxylating dehydrogenases from Sulfolobus acidocaldarius
Extremophiles
20
843-853
2016
Sulfolobus acidocaldarius MW001
27590116
1.1.1.286
685232
Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae
Biochemistry
47
4169-4180
2008
Saccharomyces cerevisiae
18321070
1.1.1.286
740000
Determinants of dual substrate specificity revealed by the crystal structure of homoisocitrate dehydrogenase from Thermus thermophilus in complex with homoisocitrate-Mg(2+)-NADH
Biochem. Biophys. Res. Commun.
478
1688-1693
2016
Thermus thermophilus
27601325
1.1.1.286
740000
Determinants of dual substrate specificity revealed by the crystal structure of homoisocitrate dehydrogenase from Thermus thermophilus in complex with homoisocitrate-Mg(2+)-NADH
Biochem. Biophys. Res. Commun.
478
1688-1693
2016
Thermus thermophilus DSM 7039
27601325
1.1.1.286
660918
Identification of a novel trifunctional homoisocitrate dehydrogenase and modulation of the broad substrate specificity through site-directed mutagenesis
Biochem. Biophys. Res. Commun.
336
596-602
2005
Deinococcus radiodurans
16139794
1.1.1.286
696220
Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae
Biochemistry
47
10809-10815
2008
Saccharomyces cerevisiae
18785753
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