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Dolichyl-phosphate-mannose-protein mannosyltransferase








Dolichyl-phosphate-mannose-protein mannosyltransferase


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dolichyl-phosphate-mannose-protein mannosyltransferase
Identifiers
EC number
2.4.1.109
CAS number
74315-99-4
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile

PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO

















In enzymology, a dolichyl-phosphate-mannose-protein mannosyltransferase (EC 2.4.1.109) is an enzyme that catalyzes the chemical reaction


dolichyl phosphate D-mannose + protein ⇌{displaystyle rightleftharpoons }rightleftharpoons dolichyl phosphate + O-D-mannosylprotein

Thus, the two substrates of this enzyme are dolichyl phosphate D-mannose and protein, whereas its two products are dolichyl phosphate and O-D-mannosylprotein.


This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase. Other names in common use include dolichol phosphomannose-protein mannosyltransferase, and protein O-D-mannosyltransferase. A human gene that codes for this enzyme is POMT1.



References[edit]






  • 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&ndash, 15. doi:10.1111/j.1432-1033.1980.tb04526.x. PMID 6989607..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  • 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&ndash, 23. doi:10.1111/j.1432-1033.1980.tb04527.x. PMID 6445267.












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