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

BRENDA support

Literature summary for 2.4.1.83 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

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

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