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Literature summary for 4.1.3.30 extracted from

  • Liu, S.; Lu, Z.; Han, Y.; Melamud, E.; Dunaway-Mariano, D.; Herzberg, O.
    Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution (2005), Biochemistry, 44, 2949-2962.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of the inactive mutant C123S MICL in complex with isocitrate are obtained at room temperature by vapor diffusion in hanging drops. A crystal of C123S MICL in complex with pyruvate and succinate was obtained by overnight incubation of a C123S MICL/isocitrate complex crystal in a solution containing 35% PEG3350, 100 mM pyruvate and 100 mM succinate. This crystal also belongs to space group C2 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P77541
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate a catalytic mechanism is proposed that involves an R-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methyl-isocitrate Escherichia coli Pyruvate + succinate
-
?

Synonyms

Synonyms Comment Organism
MICL
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
19
-
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
Escherichia coli