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Ligand (2R,3S)-2-ethyl-3-methylmalate Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C7 H1 2 O5
(2R,3S)-2-ethyl-3-methylmalate
HKEITEHXIPIELZ-CLZZGJSISA-N
(2R)-ethyl-(3S)-methyl malate, (2R)-ethyl-(3S)-methylmalate
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (3 results)
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(2R,3S)-2-ethyl-3-methylmalate + H2O = ?
-
(2R)-ethyl-(3S)-methyl malate = 2-oxobutanoate + propanoate
-
(2R)-ethyl-(3S)-methylmalate = ?
-
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (6 results)
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63
-
wild type enzyme, at pH 7.5 and 25°C
63
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
KM Value (8 results)
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1.17
-
wild type enzyme, at pH 7.5 and 25°C
1.17
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
References & Links Literature References (3)
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Diversity of function in the isocitrate lyase enzyme superfamily: the Dianthus caryophyllus petal death protein cleaves alpha-keto and alpha-hydroxycarboxylic acids
2005
Lu, Z.; Feng, X.; Song, L.; Han, Y.; Kim, A.; Herzberg, O.; Woodson, W.R.; Martin, B.M.; Mariano, P.S.; Dunaway-Mariano, D.
Biochemistry
44
16365-16376
Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method
2008
Joosten, H.J.; Han, Y.; Niu, W.; Vervoort, J.; Dunaway-Mariano, D.; Schaap, P.J.
Proteins
70
157-166
Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member
2009
Narayanan, B.; Niu, W.; Joosten, H.J.; Li, Z.; Kuipers, R.K.; Schaap, P.J.; Dunaway-Mariano, D.; Herzberg, O.
J. Mol. Biol.
386
486-503
Links to other databases for (2R,3S)-2-ethyl-3-methylmalate