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

BRENDA support

Literature summary for 4.3.2.10 extracted from

  • Liebold, C.; List, F.; Kalbitzer, H.R.; Sterner, R.; Brunner, E.
    The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy (2010), Protein Sci., 19, 1774-1782 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
T78M mutant enzyme with reduced catalytic activity Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X0C6 AND Q9X0C8 Q9X0C6: subunit HisF, Q9X0C8: subunit HisH
-
Thermotoga maritima ATCC 43589 Q9X0C6 AND Q9X0C8 Q9X0C6: subunit HisF, Q9X0C8: subunit HisH
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermotoga maritima

Subunits

Subunits Comment Organism
dimer the enzyme is a 1:1 complex of the glutaminase subunit HisH and the cyclase subunit HisF. Subunit HisF contains three distinct internal cavities, which can be identified by xenon-induced chemical shift changes of the neighboring amino acid residues. Two of these cavities are located at the active site at opposite ends of the substrate N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide binding groove. The third cavity is located in the interior of the central beta-barrel of HisF and overlaps with the putative ammonia transport channel Thermotoga maritima

Synonyms

Synonyms Comment Organism
ImGP synthase
-
Thermotoga maritima