|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: dolichyl-phosphate-mannose--protein mannosyltransferase
Enzyme Commission Synonyms: dolichol phosphomannose-protein mannosyltransferase, protein O-D-mannosyltransferase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -95.1897 [Latendresse13]
Enzyme Commission Summary:
The enzyme transfers mannosyl residues to the hydroxy group of serine or threonine residues, producing cell-wall mannoproteins. It acts only on long-chain α-dihydropolyprenyl derivatives, larger than C35.
Relationship Links: BRENDA:EC:220.127.116.11 , ENZYME:EC:18.104.22.168 , IUBMB-ExplorEnz:EC:22.214.171.124 , UniProt:RELATED-TO:P31382 , UniProt:RELATED-TO:P33775 , UniProt:RELATED-TO:P46971 , UniProt:RELATED-TO:P47190
Babczinski80: Babczinski P, Haselbeck A, Tanner W (1980). "Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme." Eur J Biochem 105(3);509-15. PMID: 6989607
Palamarczyk80: Palamarczyk G, Lehle L, Mankowski T, Chojnacki T, Tanner W (1980). "Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives." Eur J Biochem 105(3);517-23. PMID: 6445267
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