| chitobiosyldiphosphodolichol beta-mannosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.142 | ||||||||
| CAS no. | 83380-85-2 | ||||||||
| 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 chitobiosyldiphosphodolichol beta-mannosyltransferase (EC 2.4.1.142) is an enzyme that catalyzes the chemical reaction
- GDP-mannose + chitobiosyldiphosphodolichol GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol
Thus, the two substrates of this enzyme are GDP-mannose and chitobiosyldiphosphodolichol, whereas its two products are GDP and beta-1,4-D-mannosylchitobiosyldiphosphodolichol.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is GDP-mannose:chitobiosyldiphosphodolichol beta-D-mannosyltransferase. Other names in common use include guanosine diphosphomannose-dolichol diphosphochitobiose, mannosyltransferase, and GDP-mannose-dolichol diphosphochitobiose mannosyltransferase. This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.
References
- Sharma CB, Lehle L, Tanner W (1982). "Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast". Eur. J. Biochem. 126 (2): 319–25. doi:10.1111/j.1432-1033.1982.tb06781.x. PMID 6215245.
- Takahashi T, Honda R, Nishikawa Y (2000). "Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1". Glycobiology. 10 (3): 321–7. doi:10.1093/glycob/10.3.321. PMID 10704531.