Information on EC 2.4.1.285 - UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase

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The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
2.4.1.285
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RECOMMENDED NAME
GeneOntology No.
UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + ribostamycin = UDP + 2'''-acetyl-6'''-hydroxyneomycin C
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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neomycin biosynthesis
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Neomycin, kanamycin and gentamicin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:ribostamycin N-acetylglucosaminyltransferase
Involved in biosynthesis of the aminoglycoside antibiotic neomycin. Requires a divalent metal ion, optimally Mg2+, Mn2+ or Co2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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NeoK is a glycosyltransferase that catalyzes the retaining glycosylation of ribostamycin with UDP-GlcNAc as a sugar donor
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + ribostamycin
UDP + 2'''-acetyl-6'''-hydroxyneomycin C
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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about 55% residual activity in the presence of 2 mM
Co2+
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about 90% residual activity in the presence of 2 mM
EDTA
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about 20% residual activity in the presence of 10 mM
Ni2+
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about 80% residual activity in the presence of 2 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography, Superdex Hi-Load 200 gel filtration, and Mono Q column chromatography
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purified to homogeneity by DEAE Sepharose column chromatography, gel filtration, and MonoQ column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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