Glycosyltransferase DesVII
| Glycosyltransferase DesVII | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.277 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glycosyltransferase DesVII (EC 2.4.1.277, DesVII) is an enzyme with systematic name dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-alpha-D-glucosyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction
- dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide dTDP + 10-deoxymethymycin
DesVII is the glycosyltransferase responsible for the attachment of TDP-D-desosamine to macrolactones of varied ring sizes.
References
[edit]- ^ Borisova SA, Liu HW (September 2010). "Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway". Biochemistry. 49 (37): 8071–84. doi:10.1021/bi1007657. PMC 2939310. PMID 20695498.
- ^ Borisova SA, Kim HJ, Pu X, Liu HW (July 2008). "Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications". ChemBioChem. 9 (10): 1554–8. doi:10.1002/cbic.200800155. PMC 4400176. PMID 18548476.
- ^ Hong JS, Park SJ, Parajuli N, Park SR, Koh HS, Jung WS, Choi CY, Yoon YJ (January 2007). "Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation". Gene. 386 (1–2): 123–30. doi:10.1016/j.gene.2006.08.021. PMID 17049185.
External links
[edit]- Glycosyltransferase+DesVII at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
