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Literature summary for 2.4.1.83 extracted from

  • Kruszewska, J.S.; Perlinska-Lenart, U.; Palamarczyk, G.
    Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei (1996), Acta Biochim. Pol., 43, 397-401.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme is activated by cAMP-dependent protein kinase Trichoderma reesei

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Trichoderma reesei 16020
-

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme contains a potential site for phosphorylation by cAMP-dependent protein kinase Trichoderma reesei

Purification (Commentary)

Purification (Comment) Organism
one-step purification Trichoderma reesei

Storage Stability

Storage Stability Organism
during solubilization the enzyme is stabilized by the presence of lipophilic substrate dilochylphosphate and phospholipids as well as by protease inhibitors Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDPmannose + dolichyl phosphate
-
Trichoderma reesei GDP + dolichyl D-mannosyl phosphate
-
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