KEGG   ENZYME: 2.4.1.277
Entry
EC 2.4.1.277                Enzyme                                 
Name
10-deoxymethynolide desosaminyltransferase;
glycosyltransferase DesVII;
DesVII
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-alpha-D-glucosyltransferase
Reaction(IUBMB)
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin [RN:R06460]
Reaction(KEGG)
R06460;
(other) R06461
Substrate
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose [CPD:C11911];
10-deoxymethynolide [CPD:C11993]
Product
dTDP [CPD:C00363];
10-deoxymethymycin [CPD:C11994]
Comment
DesVII is the glycosyltransferase responsible for the attachment of dTDP-D-desosamine to 10-deoxymethynolide or narbonolide during the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in the bacterium Streptomyces venezuelae. Activity requires an additional protein partner, DesVIII.
History
EC 2.4.1.277 created 2011, modified 2014
Pathway
ec00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K16004  narbonolide/10-deoxymethynolide desosaminyltransferase
Genes
SGXH4W23_25525
Reference
1  [PMID:20695498]
  Authors
Borisova SA, Liu HW
  Title
Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway.
  Journal
Biochemistry 49:8071-84 (2010)
DOI:10.1021/bi1007657
  Sequence
Reference
2  [PMID:18548476]
  Authors
Borisova SA, Kim HJ, Pu X, Liu HW
  Title
Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications.
  Journal
Chembiochem 9:1554-8 (2008)
DOI:10.1002/cbic.200800155
Reference
3  [PMID:17049185]
  Authors
Hong JS, Park SJ, Parajuli N, Park SR, Koh HS, Jung WS, Choi CY, Yoon YJ
  Title
Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation.
  Journal
Gene 386:123-30 (2007)
DOI:10.1016/j.gene.2006.08.021
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.277
IUBMB Enzyme Nomenclature: 2.4.1.277
ExPASy - ENZYME nomenclature database: 2.4.1.277
BRENDA, the Enzyme Database: 2.4.1.277
LinkDB

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