HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 2.4.1.278 - 3-alpha-mycarosylerythronolide B desosaminyl transferase
for references in articles please use BRENDA:EC2.4.1.278
Word Map on EC 2.4.1.278
- 2.4.1.278
- erythromycin
- glycosyltransferases
- erythraea
-
polyketide
-
saccharopolyspora
-
macrolide
- streptomyces
-
d-desosamine
-
deoxysugars
-
erythromycin-producing
-
spinosyns
- antibioticus
- medicine
-
combinatorial
-
14-membered
-
auxiliary
-
6-deoxyerythronolide
-
interspecies
-
macrolactone
-
aglycone
- peucetius
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.4.1.278
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
3-alpha-mycarosylerythronolide B desosaminyl transferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dTDP-D-desosamine + 3-alpha-L-mycarosylerythronolide B = dTDP + erythromycin D
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme is involved in erythromycin biosynthesis
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
dTDP-D-desosamine + 3-alpha-L-mycarosylerythronolide B
dTDP + erythromycin D
-
-
-
-
dTDP-D-mycaminose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin M
-
the activated enzyme is capable of transferring an alternative sugar donor
-
-
?
additional information
?
-
-
no activity with: TDP-D-mycaminose, 6-deoxy-erythronolide B, 10-deoxymethynolide
-
-
-
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
-
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose i.e. dTDP-D-desosamine
-
-
?
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
-
TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose i.e. TDP-D-desosamine
product detected by HPLC. Identity is conformed via mass spectrometry and chromatographic comparison with an authentic reference standard
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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-4,6-dideoxy-alpha-D-glucopyranose + 3-alpha-mycarosylerythronolide B
dTDP + erythromycin D
-
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose i.e. dTDP-D-desosamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AKnT protein
-
the noncognate glycosyltransferase activator protein AknT, stably activates EryCIII. Addition of purified AknT to inactive EryCIII restores the activity of EryCIII in vitro
-
EryCII protein
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
3-alpha-mycarosylerythronolide B
-
pH and temperature not specified in the publication, 0.05 mM dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
-
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
0.017
3-alpha-mycarosylerythronolide B
-
pH and temperature not specified in the publication, 0.05 mM TDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
1.7
3-alpha-mycarosylerythronolide B
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
3-alpha-mycarosylerythronolide B
-
pH and temperature not specified in the publication, 0.05 mM dTDP-3-dimethylamino-4,6-dideoxy-alpha-D-glucopyranose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression of EryCIII with the GroEL/ES chaperone complex greatly enhances the expression of soluble EryCIII protein
-
expression in Escherichia coli BL21(DE3) as a C-terminal His6 fusion protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
potential use to make unnatural macrolides for use as antibacterial
medicine
-
the activated enzyme is capable of transferring an alternative unnatural sugar donor. Because the desosamine sugar contacts the 50S subunit of ribosome, the discovery that an unnatural sugar can be transferred has implications for the synthesis of new erythromycin derivatives with improved properties. Reconstitute of the activity of EryCIII in vitro for the synthesis of unnatural macrolides
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.278)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
