Information on EC 2.6.1.101 - L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.101
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RECOMMENDED NAME
GeneOntology No.
L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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kanamycin biosynthesis
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Neomycin, kanamycin and gentamicin biosynthesis
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paromamine biosynthesis I
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paromamine biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.100, L-glutamine:2-deoxy-scyllo-inosose aminotransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene btrR
UniProt
Manually annotated by BRENDA team
gene neoB, encoded in the neomycin biosynthetic gene cluster
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
show the reaction diagram
additional information
?
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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
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no inhibition by gabaculine, i.e. 3-amino-2,3-dihydrobenzoic acid, and (amino-oxy) acetic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
x * 46951, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE, x * 46801, recombinant His6-tagged enzyme, mass spectrometry
46801
x * 46951, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE, x * 46801, recombinant His6-tagged enzyme, mass spectrometry
46951
x * 46951, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE, x * 46801, recombinant His6-tagged enzyme, mass spectrometry
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
the active site of the BtrR protomer is located in a cleft between an alpha-helical N-terminus, a central alphabetaalpha-sandwich domain and an alphabeta-C-terminal domain, three-dimensional structure, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with pyridoxamine 5'-phosphate or pyridoxal 5'-phosphate, 7-14 days, X-ray diffraction structure determination and analysis at 1.7 A and 2.1 A resolution, respectively
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene btrR, expression in Escherichia coli strain BL21 (DE3) as His-tagged enzyme
gene neo-6, DNA and amino acid sequence determination and analysis, overexpression as His6-tagged enzyme in Esccherichia coli
gene neoB, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli