Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.3.1 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
Search for more literature for 4.1.3.1

Protein Variants

Protein Variants Comment Organism
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WKK7
-
-
Mycobacterium tuberculosis H37Rv P9WKK7
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homotetramer
-
 Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ICL
-
 Mycobacterium tuberculosis