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(-)-1-hydroxy-1,2,4-butanetricarboxylate, (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate, (2R,3S)-homoisocitrate, 1-hydroxy-1,2,4-butanetricarboxylate, 2(R),3(S)-homoisocitrate, 2-hydroxy-3-carboxyadipate, 3-carboxy-2-hydroxyadipate, D-homoisocitrate, homoisocitric acid, threo-DL-homoisocitrate
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4.8
-
pH 8.0, 60°C, recombinant His6-tagged mutant T71V
5.46
-
30°C, pH 7.8, A80 deletion mutant
6.9
-
pH 8.0, 60°C, recombinant His6-tagged mutant S80A
13
-
pH 8.0, 60°C, recombinant His6-tagged mutant L81P
17
-
pH 8.0, 60°C, recombinant His6-tagged wild-type enzyme
20.8
-
30°C, pH 7.8, mutant R87V
27.8
-
30°C, pH 7.8, mutant R87T
33
-
pH 8.0, 60°C, recombinant enzyme
37
-
pH 8.0, 60°C, recombinant enzyme
43
-
pH 8.0, 60°C, recombinant His6-tagged mutant L83R
45
-
pH 8.0, 60°C, recombinant His6-tagged mutant I82N
46.2
-
30°C, pH 7.8, wild-type
13.7
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1 mM NAD+
0.26
-
at pH 8.0 and 60°C
0.38
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.4
-
native enzyme, pH 7.8, 20°C
4.8
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
5.46
-
pH 7.8, 25°C, recombinant mutant A80del
6.9
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
12
-
wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
13
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
13.7
-
pH 7.8, 70°C, recombinant enzyme
17
-
pH 7.8, 36°C, recombinant enzyme
17
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
20.8
-
pH 7.8, 25°C, recombinant mutant R87V
27.8
-
pH 7.8, 25°C, recombinant mutant R87T
43
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
45
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
46
-
pH 7.8, 28°C, recombinant enzyme
46.2
-
pH 7.8, 25°C, recombinant wild-type enzyme
171
-
purified enzyme, pH 8.0, 60°C
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0.0073
-
pH 8.0, 60°C, recombinant His6-tagged wild-type enzyme
0.011
-
pH 8.0, 60°C, recombinant enzyme
0.037
-
pH 8.0, 60°C, recombinant His6-tagged mutant S80A
0.042
-
pH 8.0, 60°C, recombinant His6-tagged mutant L81P
0.17
-
pH 8.0, 60°C, recombinant His6-tagged mutant L83R
0.21
-
pH 8.0, 60°C, recombinant enzyme
0.211
-
30°C, pH 7.8, wild-type
0.46
-
pH 8.0, 60°C, recombinant His6-tagged mutant I82N
0.819
-
30°C, pH 7.8, A80 deletion mutant
0.94
-
pH 8.0, 60°C, recombinant His6-tagged mutant T71V
1
-
30°C, pH 7.8, mutant R87V
1.5
-
30°C, pH 7.8, mutant R87T
0.0183
-
6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1mM NAD+
5.9
-
at pH 8.0 and 60°C
0.0042
-
oxidate decarboxylation of homoisocitrate
0.0073
-
wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.018
-
pH 7.8, 36°C, recombinant enzyme
0.0183
-
pH 7.8, 70°C, recombinant enzyme
0.037
-
mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.042
-
mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.064
-
wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C
0.074
-
recombinant His-tagged enzyme, pH 7.8, 20°C
0.17
-
mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.211
-
pH 7.8, 25°C, recombinant wild-type enzyme
0.211
-
pH 7.8, 28°C, recombinant enzyme
0.45
-
native enzyme, pH 7.8, 20°C
0.46
-
mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C
0.819
-
pH 7.8, 25°C, recombinant mutant A80del
0.94
-
mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C
1
-
pH 7.8, 25°C, recombinant mutant R87V
1.5
-
pH 7.8, 25°C, recombinant mutant R87T
3.2
-
reductive carboxylation of alpha-ketoadipate
7.5
-
purified enzyme, pH 8.0, 60°C
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Localization of the homocitrate pathway
1968
Betterton, H.; Fjellstedt, T.; Matsuda, M.; Ogur, M.; Tate, R.
Biochim. Biophys. Acta
170
459-461
A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms
1998
Irvin, S.D.; Bhattacharjee, J.K.
J. Mol. Evol.
46
401-408
The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme involved in the fungus-specific lysine pathway
1997
Weidner, G.; Steffan, B.; Brakhage, A.A.
Mol. Gen. Genet.
255
237-247
Isocitrate lyase from Neurospora crassa. I. Purification, kinetic mechanism, and interaction with inhibitors
1974
Johanson, R.A.; Hill, J.M.; McFadden, B.A.
Biochim. Biophys. Acta
364
327-340
Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe
1988
Ye, Z.H.; Bhattacharjee, J.K.
J. Bacteriol.
170
5968-5970
Lysine biosynthesis in selected pathogenic fungi: characterization of lysine auxotrophs and the cloned LYS1 gene of Candida albicans
1992
Garrad, R.C.; Bhattacharjee, J.K.
J. Bacteriol.
174
7379-7384
Homoisocitric dehydrogenase from yeast
1970
Rowley, B.; Tucci, A.F.
Arch. Biochem. Biophys.
141
499-510
Wild-type and mutant forms of homoisocitric dehydrogenase in the yeast Saccharomycopsis lipolytica
1982
Gaillardin, C.M.; Ribet, A.M.; Heslot, H.
Eur. J. Biochem.
128
489-494
-
Homoisocitric Dehydrogenase
1971
Broquist, H.P.
Methods Enzymol.
17B
118-119
Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid
1965
Strassmann, M.; Ceci, L.N.
J. Biol. Chem.
240
4357-4361
Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase
2003
Miyazaki, J.; Kobashi, N.; Nishiyama, M.; Yamane, H.
J. Biol. Chem.
278
1864-1871
Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase
2005
Miyazaki, K.
Biochem. Biophys. Res. Commun.
331
341-346
Identification of a novel trifunctional homoisocitrate dehydrogenase and modulation of the broad substrate specificity through site-directed mutagenesis
2005
Miyazaki, K.
Biochem. Biophys. Res. Commun.
336
596-602
Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase
2007
Yamamoto, T.; Miyazaki, K.; Eguchi, T.
Bioorg. Med. Chem.
15
1346-1355
Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance
2005
Miyazaki, J.; Asada, K.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
J. Bacteriol.
187
6779-6788
Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae
2008
Lin, Y.; Volkman, J.; Nicholas, K.M.; Yamamoto, T.; Eguchi, T.; Nimmo, S.L.; West, A.H.; Cook, P.F.
Biochemistry
47
4169-4180
Thiahomoisocitrate: a highly potent inhibitor of homoisocitrate dehydrogenase involved in the alpha-aminoadipate pathway
2008
Yamamoto, T.; Eguchi, T.
Bioorg. Med. Chem.
16
3372-3376
Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae
2008
Lin, Y.; West, A.H.; Cook, P.F.
Biochemistry
47
10809-10815
Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae
2009
Lin, Y.; West, A.H.; Cook, P.F.
Biochemistry
48
7305-7312
Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit
2010
Jeyakanthan, J.; Drevland, R.M.; Gayathri, D.R.; Velmurugan, D.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Graham, D.E.
Biochemistry
49
2687-2696
Homoisocitrate dehydrogenase from Candida albicans: properties, inhibition, and targeting by an antifungal pro-drug
2013
Gabriel, I.; Vetter, N.D.; Palmer, D.R.; Milewska, M.J.; Wojciechowski, M.; Milewski, S.
FEMS Yeast Res.
13
143-155
Structure of Thermus thermophilus homoisocitrate dehydrogenase in complex with a designed inhibitor
2011
Nango, E.; Yamamoto, T.; Kumasaka, T.; Eguchi, T.
J. Biochem.
150
607-614
Antifungal activity of homoaconitate and homoisocitrate analogs
2012
Milewska, M.; Prokop, M.; Gabriel, I.; MilewskiWojciechowski, M.; Milewski, S.
Molecules
17
14022-14036
Characterization of two ?-decarboxylating dehydrogenases from Sulfolobus acidocaldarius
2016
Takahashi, K.; Nakanishi, F.; Tomita, T.; Akiyama, N.; Lassak, K.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.
Extremophiles
20
843-853
Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme
2015
Hsu, C.; West, A.H.; Cook, P.F.
Arch. Biochem. Biophys.
584
20-27
Determinants of dual substrate specificity revealed by the crystal structure of homoisocitrate dehydrogenase from Thermus thermophilus in complex with homoisocitrate-Mg(2+)-NADH
2016
Takahashi, K.; Tomita, T.; Kuzuyama, T.; Nishiyama, M.
Biochem. Biophys. Res. Commun.
478
1688-1693
Structure and function of an ancestral-type beta-decarboxylating dehydrogenase from Thermococcus kodakarensis
2017
Shimizu, T.; Yin, L.; Yoshida, A.; Yokooji, Y.; Hachisuka, S.I.; Sato, T.; Tomita, T.; Nishida, H.; Atomi, H.; Kuzuyama, T.; Nishiyama, M.
Biochem. J.
474
105-122
De novo biosynthesis of glutarate via alpha-keto acid carbon chain extension and decarboxylation pathway in Escherichia coli
2017
Wang, J.; Wu, Y.; Sun, X.; Yuan, Q.; Yan, Y.
ACS Synth. Biol.
6
1922-1930
Structure and function of an ancestral-type beta-decarboxylating dehydrogenase from Thermococcus kodakarensis
2017
Shimizu, T.; Yin, L.; Yoshida, A.; Yokooji, Y.; Hachisuka, S.; Sato, T.; Tomita, T.; Nishida, H.; Atomi, H.; Kuzuyama, T.; Nishiyama, M.
Biochem. J.
474
105-122
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