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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.109 expression in Saccharomyces cerevisiae Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.109 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
-
?
2.4.1.109 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
-
?
2.4.1.109 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

EC Number Organism UniProt Comment Textmining
2.4.1.109 Schizosaccharomyces pombe O13898
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-
2.4.1.109 Schizosaccharomyces pombe O42933
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2.4.1.109 Schizosaccharomyces pombe Q9C100
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.109 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
-
?
2.4.1.109 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
-
?
2.4.1.109 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

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