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Literature summary extracted from

  • Jongkon, N.; Chotpatiwetchkul, W.; Gleeson, M.P.
    Probing the catalytic mechanism involved in the isocitrate lyase superfamily hybrid quantum mechanical/molecular mechanical calculations on 2,3-dimethylmalate lyase (2015), J. Phys. Chem. B, 119, 11473-11484 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.30 C123S the mutation has a significant effect on its mechanism in terms of both rate and stereochemistry Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.32 Mn2+ contains Mn2+ Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.30 (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate Mycobacterium tuberculosis
-
 succinate + pyruvate
-
 ?
4.1.3.32 (2R,3S)-2,3-dimethylmalate Mycobacterium tuberculosis
-
 propanoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.30 Mycobacterium tuberculosis
-
-
-
4.1.3.32 Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.30 (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
 Mycobacterium tuberculosis succinate + pyruvate
-
 ?
4.1.3.32 (2R,3S)-2,3-dimethylmalate
-
 Mycobacterium tuberculosis propanoate + pyruvate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.3.30 2-Methylisocitrate lyase
-
 Mycobacterium tuberculosis
4.1.3.30 MICL
-
 Mycobacterium tuberculosis
4.1.3.32 DMML
-
 Mycobacterium tuberculosis