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

BRENDA support

Literature summary for 2.3.1.15 extracted from

  • Pellon-Maison, M.; Coleman, R.A.; Gonzalez-Baro, M.R.
    The C-terminal region of mitochondrial glycerol-3-phosphate acyltransferase-1 interacts with the active site region and is required for activity (2006), Arch. Biochem. Biophys., 450, 157-166.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzymes expressed in CHO cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information truncation of the C-terminal domain and characterization of the properties of the resulting mutants expressed in CHO cells. Although the mutants are overexpressed, none of them confers GPAT activity. The loss of activity is not due to the miss-targeting of the proteins. The C-terminal domain is necessary for mtGPAT1 activity, and probably contributes to catalysis or substrate binding Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane mtGPAT1 has two transmembrane domains (TMDs) (aa 472–493 and aa 576–592) with both the N- and C-termini facing the cytosol and a loop (aa 494–575) facing the intermembrane space Rattus norvegicus 31966
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
palmitoyl-CoA + sn-glycerol 3-phosphate
-
Rattus norvegicus CoA + 1-palmitoyl-sn-glycerol 3-phosphate
-
?

Synonyms

Synonyms Comment Organism
glycerol-3-phosphate acyltransferase-1
-
Rattus norvegicus
mtGPAT1
-
Rattus norvegicus