Protein Variants | Comment | Organism |
---|---|---|
D297A | site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme | Homo sapiens |
E396A | site-directed mutagenesis, the mutant shows 8% activity compared to the wild-type enzyme | Homo sapiens |
E54A | site-directed mutagenesis, inactive mutant | Homo sapiens |
R294A | site-directed mutagenesis, inactive mutant | Homo sapiens |
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 | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | - |
Homo sapiens | |
Zn2+ | complete inhibition | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetic measurements of wild-type and mutant POFUT2 | Homo sapiens | |
0.0098 | - |
GDP-fucose | pH and temperature not specified in the publication | Homo sapiens | |
0.0295 | - |
TSR4 | pH and temperature not specified in the publication | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates, but less effectiv than Mg2+ and Mn2+ | Homo sapiens | |
Mg2+ | activates | Homo sapiens | |
Mn2+ | activates, but less effectiv than Mg2+ | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP-fucose + TSR4 | Homo sapiens | - |
GDP + fucosyl-TSR4 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9Y2G5 | wild-type POFUT2 and high mannose type DelTA21-POFUT2 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
GDP-beta-L-fucose + PCQNGGSCKDQL = PCQNGGS(O-beta-L-fucosyl)-CKDQL + GDP | catalytic mechanism and substrate specificity, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GDP-fucose + TSR4 | - |
Homo sapiens | GDP + fucosyl-TSR4 | - |
? | |
GDP-fucose + TSR4 | GDP-fucose binding mode, overview. Activity with recombinant TSR4 mutants expressed in HEK293Tcells | Homo sapiens | GDP + fucosyl-TSR4 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
POFUT2 | - |
Homo sapiens |
protein O-fucosyltransferase 2 | - |
Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.4 | - |
GDP-fucose | pH and temperature not specified in the publication | Homo sapiens | |
2.4 | - |
TSR4 | pH and temperature not specified in the publication | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | POFUT2 belongs to the classical GT-B fold family of glycosyltransferases with two closely interacting Rossmann-like domains. POFUT2 shows a variation of the classical GT-B fold | Homo sapiens |
additional information | recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, 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. Structure-function analysis of POFUT2 and comparison to POFUT1 | Homo sapiens |
physiological function | protein O-fucosyltransferase 2 catalyzes the protein O-fucosylation, a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats | Homo sapiens |