Information on EC 2.4.1.277 - 10-deoxymethynolide desosaminyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces venezuelae

EC NUMBER
COMMENTARY hide
2.4.1.277
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RECOMMENDED NAME
GeneOntology No.
10-deoxymethynolide desosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methymycin, neomethymycin and novamethymycin biosynthesis
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narbomycin, pikromycin and novapikromycin biosynthesis
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Biosynthesis of 12-, 14- and 16-membered macrolides
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-alpha-D-glucosyltransferase
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
show the reaction diagram
dTDP-beta-L-mycarose + erythronolide B
dTDP + 3-alpha-L-mycarosylerythronolide B
show the reaction diagram
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reaction of EC 2.4.1.328
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?
dTDP-D-boivinose + 10-deoxymethynolide
dTDP + D-boivinosyl-10-deoxymethynolide
show the reaction diagram
dTDP-D-quinovose + 10-deoxymethynolide
dTDP + D-quinovosyl-10-deoxymethynolide
show the reaction diagram
dTDP-L-olivose + 10-deoxymethynolide
dTDP + L-olivosyl-10-deoxymethynolide
show the reaction diagram
dTDP-L-rhamnose + 10-deoxymethynolide
dTDP + L-rhamnosyl-10-deoxymethynolide
show the reaction diagram
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
show the reaction diagram
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
show the reaction diagram
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DesIII protein
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glycosyltransferase DesVII is unique among glycosyltransferases in that it requires an additional protein component, DesVIII, for activity. desVIII is important for the biosynthesis of glycosylated macrolides but can be replaced by at least one of the homologous genes from other pathways. The addition of recombinant DesVIII protein significantly improves the glycosylation efficiency of DesVII in the in vitro assay. DesVIII assists the folding of DesVII during protein production and remains tightly bound during catalysis. Although the formation of the DesVII/Des-VIII complex is essential for the catalytic activity, DesVIII is unlikely involved in catalysis directly
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DesVIII protein
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DesVIII is an auxiliary protein which enhances the transfer of TDP-D-desosamine catalyzed by DesVII glycosyltransferase in the biosynthesis of macrolide antibiotics, neomethymycin, methymycin and pikromycin, in Streptomyces venezuelae ATCC 15439. The DesVIII homologues (except for TylMIII) can functionally replace the native DesVIII for glycosylation to proceed in vivo and their functions are similar in acting as glycosyltransferase auxiliary proteins. Complementation by expressing EryCII, OleP1, and DnrQ in a desVIII deletion mutant strain restors the production of glycosylated macrolides to an approximate level of 66%, 26% and 26%, respectively, compared to self-complementation by DesVIII
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 5.83
10-deoxymethynolide
0.16 - 1.84
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0092 - 1
10-deoxymethynolide
0.0062 - 1.33
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00158 - 16.7
10-deoxymethynolide
15194
0.0034 - 0.3125
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
15195
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the calculated molecular mass of the heterodimer of the DesVII-C-His6/DesVIII-N-Stag complex is 92559 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the DesVII-C-His6/DesVIII-N-Stag complex likely exists as a trimer of heterodimers
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of desVII asaC-terminally His6-tagged protein in Escherichia coli. When affinity-tagged DesVII and DesVIII proteins are coproduced in Escherichia coli, they form a tight (alphabeta)3 complex that is at least 1000-fold more active than DesVII alone. The formation of the DesVII/DesVIII complex requires coexpression of both genes in vivo and cannot be fully achieved by mixing the individual protein components in vitro
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the recombinant DesVII protein is overproduced in Escherichia coli as a C-terminal His6-tagged fusion protein. The DesVIII protein is produced in Escherichia coli as a fusion with maltose-binding protein at its N-terminus. The fusion protein is cleaved by treatment with protease and untagged DesVIII protein is used in the assays together with DesVII
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis