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Literature summary for 2.4.1.221 extracted from

  • Valero-Gonzalez, J.; Leonhard-Melief, C.; Lira-Navarrete, E.; Jimenez-Oses, G.; Hernandez-Ruiz, C.; Pallares, M.C.; Yruela, I.; Vasudevan, D.; Lostao, A.; Corzana, F.; Takeuchi, H.; Haltiwanger, R.S.; Hurtado-Guerrero, R.
    A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2 (2016), Nat. Chem. Biol., 12, 240-246.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.221

Cloned(Commentary)

Cloned (Comment) Organism
gene profut2, recombinant expression in Pichia pastoris and secretion to the medium, partially degradation of the protein Caenorhabditis elegans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme CePOFUT2 in complex with GDP and human TSR1, X-ray diffraction structure determination and analysis Caenorhabditis elegans

Protein Variants

Protein Variants Comment Organism
G19Q site-directed mutagenesis, the mutation affects both secretion and fucosylation Caenorhabditis elegans
G19R site-directed mutagenesis, the mutation affects both secretion and fucosylation Caenorhabditis elegans
G20H site-directed mutagenesis, the mutation affects both secretion and fucosylation Caenorhabditis elegans
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 Caenorhabditis elegans
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 Caenorhabditis elegans
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 Caenorhabditis elegans
V16H site-directed mutagenesis, the mutation affects both secretion and fucosylation Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates wild-type and mutant enzymes, but has a nonessential role in catalysis. Residue R290 replaces Mn2+ function by establishing electro­static and hydrogen bond interactions with beta-phosphate Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q8WR51 gene profut2
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme CePOFUT2 in complex with GDP and human TSR1 by gel filtration Caenorhabditis elegans

Reaction

Reaction Comment Organism Reaction ID
GDP-beta-L-fucose + PCQNGGSCKDQL = PCQNGGS(O-beta-L-fucosyl)-CKDQL + GDP catalytic mechanism of isozyme POFUT2 and its preference for threonine over serine residues Caenorhabditis elegans
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme POFUT2 fucosylates threonine pref­erentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-, substrate specificity, overview Caenorhabditis elegans ?
-
 ?

Synonyms

Synonyms Comment Organism
POFUT2
-
 Caenorhabditis elegans
protein O-fucosyltransferase 2
-
 Caenorhabditis elegans

General Information

General Information Comment Organism
additional information enzyme in complex with GDP and human thrombospondin type 1 repeat shows an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the thrombospondin type 1 repeat is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex, role of interstitial water in the complex interface, water-mediated interactions, overview Caenorhabditis elegans
physiological function protein O-fucosyltransferase 2 is an essential enzyme that fucosylates serine and threonine residues of folded thrombospondin type 1 repeats Caenorhabditis elegans