ExplorEnz: EC 2.4.1.109

Your query returned 1 entry. Printable version

2.4.1.109

Accepted name:

dolichyl-phosphate-mannose—protein mannosyltransferase

Reaction:

(1) dolichyl β-D-mannosyl phosphate + L-threonyl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-threonyl-[protein]
(2) dolichyl β-D-mannosyl phosphate + L-seryl-[protein] = dolichyl phosphate + 3-O-(α-D-mannosyl)-L-seryl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

dolichol phosphomannose-protein mannosyltransferase; protein O-D-mannosyltransferase; dolichyl-phosphate-D-mannose:protein O-D-mannosyltransferase; dolichyl-phosphate-mannose-protein mannosyltransferase; dolichyl-D-mannosyl-phosphate:protein O-D-mannosyltransferase

Systematic name:

dolichyl β-D-mannosyl-phosphate:L-threonyl/L-seryl-[protein] O-D-mannosyltransferase (configuration-inverting)

Comments:

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.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 74315-99-4

References:

1.	Babczinski, P., Haselbeck, A. and Tanner, W. Yeast mannosyl transferases requiring dolichyl phosphate and dolichyl phosphate mannose as substrate. Partial purification and characterization of the solubilized enzyme. Eur. J. Biochem. 105 (1980) 509–515. [DOI] [PMID: 6989607]
2.	Palamarczyk, G., Lehle, L., Mankowski, T., Chojnacki, T. and Tanner, W. Specificity of solubilized yeast glycosyl transferases for polyprenyl derivatives. Eur. J. Biochem. 105 (1980) 517–523. [DOI] [PMID: 6445267]

[EC 2.4.1.109 created 1983, modified 2014]