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Literature summary for 4.1.3.1 extracted from

  • Shukla, H.; Kumar, V.; Singh, A.K.; Singh, N.; Kashif, M.; Siddiqi, M.I.; Yasoda Krishnan, M.; Sohail Akhtar, M.
    Insight into the structural flexibility and function of Mycobacterium tuberculosis isocitrate lyase (2015), Biochimie, 110, 73-80 .
    View publication on PubMed
Search for more literature for 4.1.3.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C41(DE3) cells Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
E423A inactive Mycobacterium tuberculosis
E423A/E424A inactive Mycobacterium tuberculosis
E423D the mutant shows about 75% of wild type enzyme activity Mycobacterium tuberculosis
E423D/E424D the mutant shows about 60% of wild type enzyme activity Mycobacterium tuberculosis
E423K inactive Mycobacterium tuberculosis
E423K/E424K inactive Mycobacterium tuberculosis
E423L inactive Mycobacterium tuberculosis
E424A inactive Mycobacterium tuberculosis
E424D the mutant shows about 70% of wild type enzyme activity Mycobacterium tuberculosis
E424K inactive Mycobacterium tuberculosis
E424L inactive Mycobacterium tuberculosis
H180A the mutation leads to the destabilization and formation of inactive monomeric enzyme Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.142
-
 threo-DL-Isocitrate wild type enzyme, at pH 7.5 and 30°C Mycobacterium tuberculosis
1.423
-
 threo-DL-Isocitrate mutant enzyme E423D, at pH 7.5 and 30°C Mycobacterium tuberculosis
1.861
-
 threo-DL-Isocitrate mutant enzyme E424D, at pH 7.5 and 30°C Mycobacterium tuberculosis
2.031
-
 threo-DL-Isocitrate mutant enzyme E423D/E424D, at pH 7.5 and 30°C Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
192000
-
 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
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Mycobacterium tuberculosis

Source Tissue

Source Tissue Comment Organism Textmining

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 4 * 48000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ICL
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.53
-
 threo-DL-Isocitrate mutant enzyme E423D/E424D, at pH 7.5 and 30°C Mycobacterium tuberculosis
8.34
-
 threo-DL-Isocitrate mutant enzyme E423D, at pH 7.5 and 30°C Mycobacterium tuberculosis
8.46
-
 threo-DL-Isocitrate mutant enzyme E424D, at pH 7.5 and 30°C Mycobacterium tuberculosis
9.78
-
 threo-DL-Isocitrate wild type enzyme, at pH 7.5 and 30°C Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function isocitrate lyase is a key enzyme of the glyoxylate shunt crucial for the survival of Mycobacterium tuberculosis in macrophages during persistent infection Mycobacterium tuberculosis