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Literature summary extracted from

  • Shukla, H.; Shukla, R.; Sonkar, A.; Pandey, T.; Tripathi, T.
    Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility (2017), Sci. Rep., 7, 1058 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.1 F345A the mutation leads to complete loss of the enzyme activity, compromises the enzyme stability, and modulates the structural dynamics and flexibility of the protein Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.3.1 200000
-
 gel filtration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.1 isocitrate Mycobacterium tuberculosis
-
 succinate + glyoxylate
-
 ?
4.1.3.1 isocitrate Mycobacterium tuberculosis H37Rv
-
 succinate + glyoxylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.1 Mycobacterium tuberculosis P9WKK7
-
-
4.1.3.1 Mycobacterium tuberculosis H37Rv P9WKK7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.1 isocitrate
-
 Mycobacterium tuberculosis succinate + glyoxylate
-
 ?
4.1.3.1 isocitrate
-
 Mycobacterium tuberculosis H37Rv succinate + glyoxylate
-
 ?
4.1.3.1 threo-DL-isocitrate
-
 Mycobacterium tuberculosis succinate + glyoxylate
-
 ?
4.1.3.1 threo-DL-isocitrate
-
 Mycobacterium tuberculosis H37Rv succinate + glyoxylate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.3.1 homotetramer
-
 Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
4.1.3.1 ICL
-
 Mycobacterium tuberculosis