Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.109 extracted from

  • Tanaka, N.; Fujita, Y.; Suzuki, S.; Morishita, M.; Giga-Hama, Y.; Shimoda, C.; Takegawa, K.
    Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe (2005), Biochem. Biophys. Res. Commun., 330, 813-820.
    View publication on PubMed
Search for more literature for 2.4.1.109

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl phosphate D-mannose + protein Schizosaccharomyces pombe O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein Schizosaccharomyces pombe O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein Schizosaccharomyces pombe O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells dolichyl phosphate + O-D-mannosylprotein
-
 ?

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe O13898
-
-
Schizosaccharomyces pombe O42933
-
-
Schizosaccharomyces pombe Q9C100
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl phosphate D-mannose + protein O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential Schizosaccharomyces pombe dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination Schizosaccharomyces pombe dolichyl phosphate + O-D-mannosylprotein
-
 ?
dolichyl phosphate D-mannose + protein O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells Schizosaccharomyces pombe dolichyl phosphate + O-D-mannosylprotein
-
 ?

Synonyms

Synonyms Comment Organism
dolichyl-phosphate-mannose--protein mannosyltransferase 1
-
 Schizosaccharomyces pombe
dolichyl-phosphate-mannose--protein mannosyltransferase 2
-
 Schizosaccharomyces pombe
dolichyl-phosphate-mannose--protein mannosyltransferase 4
-
 Schizosaccharomyces pombe
O-glycoside mannosyltransferase
-
 Schizosaccharomyces pombe
ogm1
-
 Schizosaccharomyces pombe
ogm2
-
 Schizosaccharomyces pombe
ogm4
-
 Schizosaccharomyces pombe