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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87746605 De novo biosynthesis of glutarate via alpha-keto acid carbon chain extension and decarboxylation pathway in Escherichia coli ACS Synth. Biol. 6 1922-1930 2017 Saccharomyces cerevisiae 28618222
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87746605 De novo biosynthesis of glutarate via alpha-keto acid carbon chain extension and decarboxylation pathway in Escherichia coli ACS Synth. Biol. 6 1922-1930 2017 Saccharomyces cerevisiae ATCC 204508 28618222
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87739958 Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme Arch. Biochem. Biophys. 584 20-27 2015 Saccharomyces cerevisiae 26325079
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87644539 Homoisocitric dehydrogenase from yeast Arch. Biochem. Biophys. 141 499-510 1970 Saccharomyces cerevisiae 4395693
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87660907 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
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87660918 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
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87760522 Structure and function of an ancestral-type beta-decarboxylating dehydrogenase from Thermococcus kodakarensis Biochem. J. 474 105-122 2017 Thermococcus kodakarensis 27831491
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87760522 Structure and function of an ancestral-type beta-decarboxylating dehydrogenase from Thermococcus kodakarensis Biochem. J. 474 105-122 2017 Thermococcus kodakarensis KUW1 27831491
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87685232 Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae Biochemistry 47 4169-4180 2008 Saccharomyces cerevisiae 18321070
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87696220 Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae Biochemistry 47 10809-10815 2008 Saccharomyces cerevisiae 18785753
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