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Information on EC 2.4.1.277 - 10-deoxymethynolide desosaminyltransferase
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2.4.1.277 10-deoxymethynolide desosaminyltransferaseIUBMB Comments
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.
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Word Map
- 2.4.1.277
- venezuelae
- pikromycin
- polyketide
-
deoxysugars
-
aglycone
-
macrolactone
-
d-desosamine
- methymycin
- erythromycin
- tylosin
- synthases
-
auxiliary
- tylactone
-
interspecies
-
saccharopolyspora
- medicine
- neomethymycin
-
unnatural
- l-rhamnose
-
bioconversion
- fradiae
- cassettes
- erythraea
-
erythromycin-susceptible
- faecium
-
enterococcus
- narbomycin
- aureus
-
16-membered
- glycosyltransferases
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
desvii, desvii/desviii, glycosyltransferase desvii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
macrolide glycosyltransferase DesVII
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
dTDP-beta-L-mycarose + erythronolide B
dTDP + 3-alpha-L-mycarosylerythronolide B
-
reaction of EC 2.4.1.328
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
dTDP-D-boivinose + 10-deoxymethynolide
dTDP + D-boivinosyl-10-deoxymethynolide
-
-
-
?
dTDP-D-boivinose + 10-deoxymethynolide
dTDP + D-boivinosyl-10-deoxymethynolide
-
-
-
?
dTDP-D-quinovose + 10-deoxymethynolide
dTDP + D-quinovosyl-10-deoxymethynolide
-
-
-
?
dTDP-D-quinovose + 10-deoxymethynolide
dTDP + D-quinovosyl-10-deoxymethynolide
-
-
-
?
dTDP-L-olivose + 10-deoxymethynolide
dTDP + L-olivosyl-10-deoxymethynolide
-
-
-
?
dTDP-L-olivose + 10-deoxymethynolide
dTDP + L-olivosyl-10-deoxymethynolide
-
-
-
?
dTDP-L-rhamnose + 10-deoxymethynolide
dTDP + L-rhamnosyl-10-deoxymethynolide
-
substitution with L-rhamnose results in better antibacterial activity than parent compound 10-deoxymethymycin
-
?
dTDP-L-rhamnose + 10-deoxymethynolide
dTDP + L-rhamnosyl-10-deoxymethynolide
-
substitution with L-rhamnose results in better antibacterial activity than parent compound 10-deoxymethymycin
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-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. The enzyme is involved in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in Streptomyces venezuelae
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
the enzyme is involved in biosynthesis of macrolide antibiotics
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
DesVII/DesVIII exhibits a stringent 6-deoxysugar requirement but an otherwise relaxed substrate specificity toward both TDP-sugar donor and aglycone acceptor
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose i.e. dTDP-D-desosamine (a 14-membered macrolactone ring). The formation of aglycone is observed when 10-deoxymethymycin is incubated with an excess of TDP in the presence of DesVII-C-His6/DesVIII-N-Stag. The equilibrium of the reaction strongly favors the glycosylation direction because only less than 10% of 10-deoxymethylmycin is converted to 10-deoxymethynolide after a 24 h incubation period
-
-
r
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
the enzyme is involved in biosynthesis of macrolide antibiotics
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
DesVII/DesVIII exhibits a stringent 6-deoxysugar requirement but an otherwise relaxed substrate specificity toward both TDP-sugar donor and aglycone acceptor
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
-
-
-
?
additional information
?
-
the enzyme can also recognize and process the linear precursor of its macrolactone substrate with reduced but measurable activity. The reaction is regioselective because only one singly glycosylated product is generated in each case despite the presence of multiple potential glycosylation sites. The substitution patterns nearby the glycosylation site, and not the ring conformation, are the major recognition determinants for glycosyltransferase
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-
?
additional information
?
-
the macrolide glycosyltransferase, DesVII/DesVIII, can recognize and process not only cyclic substrates of different ring size, but also a variety of linear substrates albeit with reduced, but measurable activities. When multiple hydroxyl groups are present, essentially no regiospecificity is observed for the linear substrates. Only singly glycosylated products are generated in all cases. In contrast, when cyclic substrates with multiple glycosylation sites are tested, the enzyme displays excellent regiospecificity in most cases
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-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. The enzyme is involved in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in Streptomyces venezuelae
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
the enzyme is involved in biosynthesis of macrolide antibiotics
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 10-deoxymethynolide
dTDP + 10-deoxymethymycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
-
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
the enzyme is involved in biosynthesis of macrolide antibiotics
-
-
?
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + narbonolide
dTDP + narbomycin
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DesIII protein
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
-
DesVIII protein
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
LITERATURE
IMAGE
0.06
10-deoxymethynolide
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 1.0 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
5.83
10-deoxymethynolide
pH 8.0, 29°C, cosubstrate: 10 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
0.16
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 9.1 mM 10-deoxymethynolide
1.84
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, cosubstrate: 9.1 mM 10-deoxymethynolide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0092
10-deoxymethynolide
pH 8.0, 29°C, cosubstrate: 10 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
1
10-deoxymethynolide
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 1.0 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
0.0062
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, cosubstrate: 9.1 mM 10-deoxymethynolide
1.33
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 9.1 mM 10-deoxymethynolide
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00158
10-deoxymethynolide
pH 8.0, 29°C, cosubstrate: 10 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
16.7
10-deoxymethynolide
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 1.0 mM dTDP-3-amino-4,6-dideoxy-alpha-D-glucopyranose
0.0034
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, cosubstrate: 9.1 mM 10-deoxymethynolide
0.3125
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
pH 8.0, 29°C, addition of the DesIII protein, cosubstrate: 9.1 mM 10-deoxymethynolide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme is involved in biosynthesis of macrolide antibiotics
physiological function
coexpression of glycosyltransferase DesVII and its auxiliary partner DesVIII in a Saccharopolyspora erythraea EryBV deletion mutant leads to an increased erythromycin A yield by 15% in comparison to Saccharopolyspora erythraea wild-type. DesVII/DesVIII replaced EryCIII to upload D-desosamine to C5 position of 3-O-mycarosyl erythronolide B and also in vivo attache L-mycarose, not D-desosamine to C3 position of erythronolide B with a higher activity than EryBV. Expression of DesVII in EryCIII and EryBV-CIII mutant strains partially restores the erythromycin A production, however, no erythromycin A is detected while DesVII is expressed in the EryBV mutant strain
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the calculated molecular mass of the heterodimer of the DesVII-C-His6/DesVIII-N-Stag complex is 92559 Da
additional information
-
the calculated molecular mass of the heterodimer of the DesVII-C-His6/DesVIII-N-Stag complex is 92559 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the DesVII-C-His6/DesVIII-N-Stag complex likely exists as a trimer of heterodimers
additional information
-
the DesVII-C-His6/DesVIII-N-Stag complex likely exists as a trimer of heterodimers
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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
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
LITERATURE
medicine
synthesis
medicine
the catalytic flexibility of the glycosyltransferase DesVII offers an means for creating new macrolide antibiotics. The substrate flexibility of DesVII/DesVIII is apparently extended to a wide range of linear as well as cyclic substrates. Although the yield of products is notably reduced when unnatural substrates are used, once a desired activity is identified, the catalytic efficiency of these enzymes may be fine-tuned by protein engineering. The substrate flexibility of glycosyltransferases expands the opportunities for glycodiversification to generate new glycoforms of synthetic compounds and macrolide analogues
medicine
the requirement for an additional protein component, DesVIII, for activity must be taken into consideration in the design of combinatorial biosynthetic experiments with new glycosylated macrolides
synthesis
expression of different deoxysugar biosynthetic gene cassettes and the gene encoding a substrate-flexible glycosyltransferase DesVII in Streptomyces venezuelae YJ003 mutant strain bearing a deletion of a desosamine biosynthetic (des) gene cluster. The resulting recombinants produce macrolide antibiotic YC-17 analogs possessing unnatural sugars replacing native D-desosamine. These metabolites are D-quinovosyl-10-deoxymethynolide, L-rhamnosyl-10-deoxymethynolide, L-olivosyl-10-deoxymethynolide, and D-boivinosyl-10-deoxymethynolide
synthesis
-
expression of different deoxysugar biosynthetic gene cassettes and the gene encoding a substrate-flexible glycosyltransferase DesVII in Streptomyces venezuelae YJ003 mutant strain bearing a deletion of a desosamine biosynthetic (des) gene cluster. The resulting recombinants produce macrolide antibiotic YC-17 analogs possessing unnatural sugars replacing native D-desosamine. These metabolites are D-quinovosyl-10-deoxymethynolide, L-rhamnosyl-10-deoxymethynolide, L-olivosyl-10-deoxymethynolide, and D-boivinosyl-10-deoxymethynolide
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borisova, S.A.; Zhang, C.; Takahashi, H.; Zhang, H.; Wong, A.W.; Thorson, J.S.; Liu, H.W.
Substrate specificity of the macrolide-glycosylating enzyme pair DesVII/DesVIII: opportunities, limitations, and mechanistic hypotheses
Angew. Chem. Int. Ed. Engl.
45
2748-2753
2006
Streptomyces venezuelae (Q9ZGH7)
brenda
Borisova, S.A.; Liu, H.W.
Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway
Biochemistry
49
8071-8084
2010
Streptomyces venezuelae (Q9ZGH7), Streptomyces venezuelae
brenda
Borisova, S.A.; Kim, H.J.; Pu, X.; Liu, H.W.
Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications
Chembiochem
9
1554-1558
2008
Streptomyces venezuelae (Q9ZGH7)
brenda
Hong, J.S.; Park, S.J.; Parajuli, N.; Park, S.R.; Koh, H.S.; Jung, W.S.; Choi, C.Y.; Yoon, Y.J.
Functional analysis of desVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation
Gene
386
123-130
2006
Streptomyces venezuelae (Q9ZGH7), Streptomyces venezuelae ATCC 15439 (Q9ZGH7), Streptomyces venezuelae ATCC 15439
brenda
Borisova, S.A.; Zhao, L.; Melancon III, C.E.; Kao, C.L.; Liu, H.W.
Characterization of the glycosyltransferase activity of desVII: analysis of and implications for the biosynthesis of macrolide antibiotics
J. Am. Chem. Soc.
126
6534-6535
2004
Streptomyces venezuelae (Q9ZGH7)
brenda
Kao, C.L.; Borisova, S.A.; Kim, H.J.; Liu, H.W.
Linear aglycones are the substrates for glycosyltransferase DesVII in methymycin biosynthesis: analysis and implications
J. Am. Chem. Soc.
128
5606-5607
2006
Streptomyces venezuelae (Q9ZGH7)
brenda
Wu, H.; Li, W.; Xin, C.; Zhang, C.; Wang, Y.; Ren, S.; Ren, M.; Zhao, W.; Yuan, L.; Xu, Z.; Yuan, H.; Geng, M.; Zhang, L.; Weaver, D.T.; Zhang, B.
In vivo investigation to the macrolide-glycosylating enzyme pair DesVII/DesVIII in Saccharopolyspora erythraea
Appl. Microbiol. Biotechnol.
100
2257-2266
2016
Streptomyces venezuelae (Q9ZGH7)
brenda
Shinde, P.B.; Han, A.R.; Cho, J.; Lee, S.R.; Ban, Y.H.; Yoo, Y.J.; Kim, E.J.; Kim, E.; Song, M.C.; Park, J.W.; Lee, D.G.; Yoon, Y.J.
Combinatorial biosynthesis and antibacterial evaluation of glycosylated derivatives of 12-membered macrolide antibiotic YC-17
J. Biotechnol.
168
142-148
2013
Streptomyces venezuelae (Q9ZGH7), Streptomyces venezuelae, Streptomyces venezuelae ATCC 15439 (Q9ZGH7)
brenda
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