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Literature summary extracted from

  • Li, J.; Yen, T.Y.; Allende, M.L.; Joshi, R.K.; Cai, J.; Pierce, W.M.; Jaskiewicz, E.; Darling, D.S.; Macher, B.A.; Young, W.W., Jr.
    Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains (2000), J. Biol. Chem., 275, 41476-41486.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.92 additional information site directed mutations in several Cys residues reveal that enzyme is homodimer with antiparallel orientation of catalytic domains and intersubunit disulfide bonds Cricetulus griseus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.92 Cricetulus griseus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.92 ovary
-
 Cricetulus griseus
-

Subunits

EC Number Subunits Comment Organism
2.4.1.92 More enzyme is homodimer with antiparallel orientation of catalytic domains and intersubunit disulfide bonds Cricetulus griseus