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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 1.1.1.87685539 Thiahomoisocitrate: a highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway Bioorg. Med. Chem. 16 3372-3376 2008 Saccharomyces cerevisiae 18086528
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87696350 Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae Biochemistry 48 7305-7312 2009 Saccharomyces cerevisiae 19530703
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87722569 Structure of Thermus thermophilus homoisocitrate dehydrogenase in complex with a designed inhibitor J. Biochem. 150 607-614 2011 Thermus thermophilus 21813504
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87722303 Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug FEMS Yeast Res. 13 143-155 2013 Candida albicans 23107040
Show all pathways known for 1.1.1.87Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.87722303 Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug FEMS Yeast Res. 13 143-155 2013 Candida albicans ATCC 10231 23107040
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 1.1.1.87746605 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 1.1.1.87760522 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
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