Information on EC 2.4.1.283 - 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
2.4.1.283
-
RECOMMENDED NAME
GeneOntology No.
2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + 2-deoxystreptamine = UDP + 2'-N-acetylparomamine
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
kanamycin biosynthesis
-
-
paromamine biosynthesis I
-
-
paromamine biosynthesis II
-
-
Neomycin, kanamycin and gentamicin biosynthesis
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-alpha-D-glucosamine [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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 + 2-deoxystreptamine
UDP + 2'-N-acetylparomamine
show the reaction diagram
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a poor amount is isolated using Ni-NTA chromatography. The cell-free extract of Escherichia coli expressing NeoD is used for enzymatic assays
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-expressed with molecular chaperone GroES and GroEL in Escherichia coli BL21(DE3) cells
-
expressed as a His-tagged fusion protein in Escherichia coli
-
KanF cannot be functionally expressed in Escherichia coli
-