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

BRENDA support

Literature summary extracted from

  • Schutzbach, J.S.; Zimmerman, J.W.; Forsee, W.T.
    The purification and characterization of recombinant yeast dolichyl-phosphate-mannose synthase. Site-directed mutagenesis of the putative dolichol recognition sequence (1993), J. Biol. Chem., 268, 24190-24196.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.83 I253N higher value for the apparent Km-value for dolichyl phosphate when assayed in detergent solution, mutation has no effect on Km-value when the enzyme is reconstituted with phosphatidylethanolamine Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.83 0.0015
-
 GDPmannose wild-type enzyme assayed in solution of Nonidet P-40 Saccharomyces cerevisiae
2.4.1.83 0.0025
-
 dolichyl phosphate wild-type enzyme reconstituted with phosphatidylethanolamine Saccharomyces cerevisiae
2.4.1.83 0.0027
-
 dolichyl phosphate wild-type enzyme reconstituted with phosphatidylethanolamine Saccharomyces cerevisiae
2.4.1.83 0.0106
-
 dolichyl phosphate wild-type enzyme assayed in solution of Nonidet P-40 Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.83 Saccharomyces cerevisiae
-
 recombinant enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.83
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.83 GDPmannose + dolichyl phosphate
-
 Saccharomyces cerevisiae GDP + dolichyl D-mannosyl phosphate
-
 ?