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Literature summary for 5.3.1.9 extracted from

  • Anand, K.; Mathur, D.; Anant, A.; Garg, L.C.
    Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv (2010), Acta Crystallogr. Sect. F, 66, 490-497.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.1.9

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 1.2 M ammonium sulfate pH 8.5 (0.1 M HEPES) and 5% (v/v) glycerol at 10°C Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
G157Y the mutation results in a complete loss of activity Mycobacterium tuberculosis
T211A the mutant shows decreased activity with higher Km compared with that of the wild type protein Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN69
-
-
Mycobacterium tuberculosis H37Rv P9WN69
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate
-
 Mycobacterium tuberculosis D-fructose 6-phosphate
-
 ?
D-glucose 6-phosphate
-
 Mycobacterium tuberculosis H37Rv D-fructose 6-phosphate
-
 ?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
PGI
-
 Mycobacterium tuberculosis
Phosphoglucose isomerase
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator Mycobacterium tuberculosis