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Literature summary 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

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

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.83 Trichoderma reesei
-
-
-

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.83 one-step purification Trichoderma reesei

Storage Stability

EC Number Storage Stability Organism
2.4.1.83 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)

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