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2.4.1.221: peptide-O-fucosyltransferase

This is an abbreviated version!
For detailed information about peptide-O-fucosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.221

Reaction

GDP-beta-L-fucose
+
PCQNGGSCKDQL
=
PCQNGGS(O-beta-L-fucosyl)-CKDQL
 +
GDP

Synonyms

alpha-6-fucosyltransferase, At3g05320, AtOFT1, core alpha6FucT, fucosyltransferase, guanosine diphosphofucose-glycoprotein, FUT2, GDP-fucose glycoprotein fucosyltransferase, GDP-fucose protein O-fucosyltransferase, GDP-fucose protein O-fucosyltransferase 1, GDP-fucose protein O-fucosyltransferase 2, GDP-fucose:polypeptide fucosyltransferase, GDP-L-fucose-glycoprotein fucosyltransferase, GDP-L-fucose:polypeptide fucosyltransferase, glycoprotein fucosyltransferase, guanosine diphosphofucose-glycoprotein fucosyltransferase, N-acetyl-beta-D-glucosaminide alpha1-->6-fucosyltransferase, N-glycan alpha-6-fucosyltransferase, O-fucosyltransferase, O-fucosyltransferase 1, O-fucosyltransferase O-fut 1, O-fucosyltransferase SPINDLY, O-fucT-1, O-fut1, OFUT1, OFUTI, Pofut1, POFUT2, protein O-fucosyltransferase 1, protein O-fucosyltransferase 2, protein O-fucosyltransferases 1, protein O-fucosyltransferases 2, SPY, TGGT1_273550

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.221 peptide-O-fucosyltransferase

Engineering

Engineering on EC 2.4.1.221 - peptide-O-fucosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D242A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows about 10% increased activity compared to the wild-type enzyme
D244A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
D309N
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F199A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F261A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F357A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
G19Q
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G19R
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G20H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
N43A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows highly reduced activity compared to the wild-type enzyme
R240A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R240K
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R298K/R299K
site-directed mutagenesis, the mutant enzyme is stable against proteolysis and similarly active as the wild-type. The mutant enzymes is capable of fucosylating TSRs not only of group 1 but also of group 2, it not only recognizes and reacts with TSRs showing slightly different structures but also accepts TSRs with very low sequence identity. Residue Glu52 of mutant CePOFUT is the catalytic base
R40A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
S15D
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduc­tion in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
S15Q
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduc­tion in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
V16H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
W245A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
R254A
-
expression of a mutant, Ofut1R245A, lacking fucosyltransferase activity, rescues the requirement for Ofut1 in embryonic neurogenesis. Lack of requirement for O-fucosylation is further supported by the absence of embryonic phenotypes in Gmd mutants, which lack all forms of fucosylation. Requirements for O-fucose during imaginal development are evaluated by characterizing clones of cells expressing only Ofut1R245A. These clones phenocopy fringe mutant clones, indicating that the absence of O-fucose is functionally equivalent to the absence of elongated O-fucose
R275A
Drosophila sp. (in: flies)
-
is catalytically dead. Ofut1 and mutant both bind the Notch extracellular domain, and expression of the mutant in cultured cells can increase both the amount and the ligand-binding activity of secreted Notch extracellular domain. Complete loss of ofut1 activity results in a strong phenotype mimicking a loss of Notch activity that is rescued to larval viability by the expression of mutant R275A, it rescues Notch receptor activity in these ofut1 mutant cells and leads to phenotypes mimicking a loss of fringe activity
D297A
site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme
E396A
site-directed mutagenesis, the mutant shows 8% activity compared to the wild-type enzyme
E54A
site-directed mutagenesis, inactive mutant
R294A
site-directed mutagenesis, inactive mutant
W273a
site-directed mutagenesis, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A
R245A
S1726A
-
mutant protein shows no activity, loss of O-fucosylation causes a gain of function for muscle agrin such that it stimulates acetylcholine receptors, clustering and MuSK phosphorylation in cultured myotubes at levels normally only found with the neural splice form
additional information