Information on EC 2.6.1.100 - L-glutamine:2-deoxy-scyllo-inosose aminotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.100
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RECOMMENDED NAME
GeneOntology No.
L-glutamine:2-deoxy-scyllo-inosose aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine
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:2-deoxy-scyllo-inosose aminotransferase
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.101, L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene btrR encoded in the butirosin cluster
UniProt
Manually annotated by BRENDA team
no activity in Streptomyces lividans
strain TK24
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Manually annotated by BRENDA team
gene btrS or alloG
UniProt
Manually annotated by BRENDA team
gene tbmB; gene tbmB
UniProt
Manually annotated by BRENDA team
gene neo6
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-
Manually annotated by BRENDA team
gene btrS, neoB, nemB, neo6, neoS, or nmcS
SwissProt
Manually annotated by BRENDA team
gene btrS, neoB, nemB, neo6, neoS, or nmcS
SwissProt
Manually annotated by BRENDA team
gene neoB, encoded in the neomycin biosynthetic gene cluster
SwissProt
Manually annotated by BRENDA team
; gene tbmBr
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Manually annotated by BRENDA team
gene btrS, rbmB, rbcS, or ribS; gene btrS
SwissProt
Manually annotated by BRENDA team
gene btrS, rbmB, rbcS, or ribS; gene btrS
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
BtrR has a fold characteristic of the aspartate aminotransferase family and is a member of the class of aminotransferases that function primarily in the biosynthesis of secondary metabolites, SMAT, i.e. the secondary metabolite aminotransferases subfamily
malfunction
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disruption mutant strain HN4 is completey devoid of neomycin production
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 + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
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 + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
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
50000
2 * 50000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 50714, mass spectrometry, 2 * 50703, sequence calculation
50703
2 * 50000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 50714, mass spectrometry, 2 * 50703, sequence calculation
50714
2 * 50000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 50714, mass spectrometry, 2 * 50703, sequence calculation
97000
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme compplexed 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 BL 21 (DE3) by cobalt affinity chromatography, gel filtration, and anion exchange chromatography
recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of analogous gene kanB from Streptomyces kanamyceticus, ATCC 12853, in Streptomyces fradiae strain HN4, that has a disruption in gene neo6, results in functional complementation of the 2-deoxystreptamine biosynthesis in stran HN4
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gene btrR, expression in Escherichia coli strain BL21 (DE3) as His-tagged enzyme
gene btrR, recombinant expression of His-tagged BtrR in Escherichia coli strain BL 21 (DE3)
gene btrS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Escherichia coli strain JM109
gene kanB, expression in and functional complementation of Streptomyces fradiae strain HN4, that has a disruption in gene neo6, an analogue to gene kanB
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gene neoB, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli
gene tbmB, expression in Escherichia coli strain BL21(DE3)