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

BRENDA support

Literature summary extracted from

  • Kurnasov, O.; Luk, H.; Roberts, M.; Stec, B.
    Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima (2013), Acta Crystallogr. Sect. D, 69, 1808-1817.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.74 structure shows a conserved motif of sugar nucleotide transferases (COG1213) with a structurally reinforced C-terminal Cys bonded to the core of the protein. During catalysis, the conserved Asp107 serves as an electrostatic anchor to which the metal ion (most likely Mg2+) binds. Upon binding, the triphosphate group of the nucleotide interacts with a metal ion as well as the phosphate of the inositol. The O atom of the inositol phosphate group that is polarized by this interaction attacks the triphosphate and causes its cleavage to release the diphosphate group. Lys24 stabilizes the developing negative charge in the transition state and Arg14 serves as a release agent Thermotoga maritima

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.74 soluble protein may transiently associate with its membrane-embedded partner phospho-DIP synthase Thermotoga maritima
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.74 Thermotoga maritima G4FFF4
-
-
2.7.7.74 Thermotoga maritima DSM 3109 G4FFF4
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.74 Tmari_1425
-
Thermotoga maritima