Information on EC 2.4.1.278 - 3-alpha-mycarosylerythronolide B desosaminyl transferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.278
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RECOMMENDED NAME
GeneOntology No.
3-alpha-mycarosylerythronolide B desosaminyl transferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-D-desosamine + 3-alpha-L-mycarosylerythronolide B = dTDP + erythromycin D
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of 12-, 14- and 16-membered macrolides
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Biosynthesis of antibiotics
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erythromycin D biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
dTDP-3-dimethylamino-3,4,6-trideoxy-alpha-D-glucopyranose:3-alpha-mycarosylerythronolide B 3-dimethylamino-3,4,6-trideoxy-beta-D-glucosyltransferase
The enzyme is involved in erythromycin biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reaction of EC 2.4.1.277
UniProt
Manually annotated by BRENDA team
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-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
show the reaction diagram
dTDP-D-desosamine + 3-alpha-L-mycarosylerythronolide B
dTDP + erythromycin D
show the reaction diagram
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dTDP-D-mycaminose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin M
show the reaction diagram
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the activated enzyme is capable of transferring an alternative sugar donor
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?
additional information
?
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no activity with: TDP-D-mycaminose, 6-deoxy-erythronolide B, 10-deoxymethynolide
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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
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
show the reaction diagram
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dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose i.e. dTDP-D-desosamine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AKnT protein
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the noncognate glycosyltransferase activator protein AknT, stably activates EryCIII. Addition of purified AknT to inactive EryCIII restores the activity of EryCIII in vitro
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EryCII protein
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glycosyltransferase activator protein EryCII activates EryCIII. EryCIII treated with EryCII is catalytically active, effecting transfer of desosamine to 3-alpha-mycarosylerythronolide. The untreated EryCIII sample shows no activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
3-alpha-mycarosylerythronolide B
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pH and temperature not specified in the publication, 0.05 mM dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 1.7
3-alpha-mycarosylerythronolide B
1.7
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
Saccharopolyspora erythraea
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pH 8.0, 25°C, in the presence og 0.001 mM EryC and 1 mM of each substrate, more than 300 turnovers are observed in 2.5 min, indicating that the kcat must be greater than 100/min. This is one of the highest turnover numbers reported for an antibiotic glycosyl transferase
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
3-alpha-mycarosylerythronolide B
Saccharopolyspora erythraea
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pH and temperature not specified in the publication, 0.05 mM dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
19514
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, activity of concentrated enzyme stored overnight is more than 3 times lower than that of freshly purified enzyme.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression of EryCIII with the GroEL/ES chaperone complex greatly enhances the expression of soluble EryCIII protein
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expression in Escherichia coli BL21(DE3) as a C-terminal His6 fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine