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2.4.1.198: phosphatidylinositol N-acetylglucosaminyltransferase

This is an abbreviated version!
For detailed information about phosphatidylinositol N-acetylglucosaminyltransferase, go to the full flat file.

Word Map on EC 2.4.1.198

Reaction

UDP-N-acetyl-alpha-D-glucosamine
+
1-phosphatidyl-1D-myo-inositol
=
UDP
+
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

Synonyms

acetyl-D-glucosaminyltransferase, uridine diphosphoacetylglucosamine alpha1,6-, afpig-a, Down syndrome critical region protein 5, DR437w, Dscr5, glycosylphosphatidylinositol N-acetylglucosaminyltransferase complex, glycosylphosphatidylinositol-N-acetylglucosaminyltransferase, GntA, GPI-GlcNAc transferase, GPI-GnT, GPI-N-acetylglucosaminyltransferase, GPI-N-acetylglucosaminyltransferase complex, GPI1, GPI15, GPI19, GPI2, GPI3, phosphatidylinositol N-acetylglucosaminyltransferase subunit A, phosphatidylinositol/UDP-GlcNAc:GlcNAc transferase, PIG-A, PigA, UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase, uridine diphosphoacetylglucosamine alpha1,6-acetyl-D-glucosaminyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.198 phosphatidylinositol N-acetylglucosaminyltransferase

Cofactor

Cofactor on EC 2.4.1.198 - phosphatidylinositol N-acetylglucosaminyltransferase

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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
enzyme binding structure analysis, overview. The variable conformations of loop beta4-beta5 and helix alphaG correlate well with the structural flexibility required for substrate entrance to the Re side of FAD