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Literature summary for 2.4.1.221 extracted from

  • Chen, C.I.; Keusch, J.J.; Klein, D.; Hess, D.; Hofsteenge, J.; Gut, H.
    Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation (2012), EMBO J., 31, 3183-3197.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Inhibitors Comment Organism Structure
EDTA
-
Homo sapiens
Zn2+ complete inhibition Homo sapiens

KM Value [mM]

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

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GDP-fucose + TSR4 Homo sapiens
-
GDP + fucosyl-TSR4
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y2G5 wild-type POFUT2 and high mannose type DelTA21-POFUT2
-

Reaction

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 and Products (Substrate)

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

Synonyms Comment Organism
POFUT2
-
Homo sapiens
protein O-fucosyltransferase 2
-
Homo sapiens

Turnover Number [1/s]

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

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