Biology:Glycosyltransferase DesVII
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Short description: Class of enzymes
| Glycosyltransferase DesVII | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] dTDP + 10-deoxymethymycin
DesVII is the glycosyltransferase responsible for the attachment of TDP-D-desosamine to macrolactones of varied ring sizes.
References
- ↑ "Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway". Biochemistry 49 (37): 8071–84. September 2010. doi:10.1021/bi1007657. PMID 20695498.
- ↑ "Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications". ChemBioChem 9 (10): 1554–8. July 2008. doi:10.1002/cbic.200800155. PMID 18548476.
- ↑ "Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation". Gene 386 (1-2): 123–30. January 2007. doi:10.1016/j.gene.2006.08.021. PMID 17049185.
External links
- Glycosyltransferase+DesVII at the US National Library of Medicine Medical Subject Headings (MeSH)
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