Literature summary for 2.4.1.92 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.

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Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Cricetulus griseus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
ovary	-	Cricetulus griseus	-

Subunits

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

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Release 2023.1 (January 2023)