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L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
additional information
?
-
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
r
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
additional information
?
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BtrR accepts four different carbocyclic substrates, 2-deoxy-scyllo-inosose, 2-deoxy-scyllo-inosamine, a ino-dideoxyscyllo-inosose, and 2-deoxysteptamine, requiring the binding site in the enzyme to have some flexibility. NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101. The existence of the closed conformation contributes to reaction type specificity within the aspartate aminotransferase family
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-
?
additional information
?
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coupled assays of TbmB with BtrC and myo-inositol dehydrogenase are performed
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-
?
additional information
?
-
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coupled assays of TbmB with BtrC and myo-inositol dehydrogenase are performed
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-
?
additional information
?
-
-
purified Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101
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-
?
additional information
?
-
NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101
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-
?
additional information
?
-
-
NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101
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-
?
additional information
?
-
NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101
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-
?
additional information
?
-
-
purified Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101
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-
?
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L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
additional information
?
-
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
r
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
L-glutamine + 2-deoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxy-scyllo-inosamine
-
-
-
?
additional information
?
-
-
purified Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101
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?
additional information
?
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purified Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101
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?
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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
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Neo-6 is the enzyme catalysing the transamination of 2-deoxy-scyllo-inosose, DOI, using L-glutamine as an amino donor to produce 2-deoxyscyllo-inosamine as required for 2-deoxystreptamine biosynthesis. Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101, the aglycon in neomycins, overview
metabolism
the aminotransferase BtrR is involved in the biosynthesis of butirosin
metabolism
the enzyme catalyses the transamination of 2-deoxy-scyllo-inosose to give 2-deoxy-scyllo-inosamine, an intermediate in the biosynthesis of 2-deoxystreptamine, biosynthetic pathway of 2-deoxystreptamine, overview
metabolism
the enzyme is involved in the biosynthesis of 2-deoxystreptamine (DOS)-containing aminoglycoside neomycin. NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101
metabolism
the enzyme is involved in the biosynthesis of kanamycin
metabolism
the enzyme is involved in the biosynthesis of neomycin
metabolism
the enzyme is involved in the biosynthesis of ribostamycin
metabolism
the enzyme is involved in tobramycin biosynthesis catalyzing the second step of the 2-deoxystreptamine biosynthetic pathway, 2-deoxystreptamine is a subunit of tobramycin, overview
metabolism
-
the enzyme is involved in the biosynthesis of ribostamycin
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metabolism
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the enzyme is involved in the biosynthesis of kanamycin
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metabolism
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Neo-6 is the enzyme catalysing the transamination of 2-deoxy-scyllo-inosose, DOI, using L-glutamine as an amino donor to produce 2-deoxyscyllo-inosamine as required for 2-deoxystreptamine biosynthesis. Neo-6 also catalyses the amino transfer from L-glutamine to 3-amino-2,3-dideoxy-scyllo-inosose to produce 2-deoxystrepamine, EC 2.6.1.101, the aglycon in neomycins, overview
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metabolism
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the enzyme is involved in the biosynthesis of neomycin
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metabolism
-
the enzyme is involved in the biosynthesis of 2-deoxystreptamine (DOS)-containing aminoglycoside neomycin. NeoB also shows L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-streptamine, EC 2.6.1.101
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metabolism
-
the enzyme is involved in the biosynthesis of neomycin
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metabolism
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the enzyme catalyses the transamination of 2-deoxy-scyllo-inosose to give 2-deoxy-scyllo-inosamine, an intermediate in the biosynthesis of 2-deoxystreptamine, biosynthetic pathway of 2-deoxystreptamine, overview
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physiological function
BtrR catalyzes the synthesis of 2-deoxystreptamine, which is the common aglycone of a class of aminoglycoside antibiotics, of which many are clinically important aminoglycosides like kanamycin, neomycin, gentamicin and butirosin
physiological function
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kanB functions as 2-deoxy-scyllo-inosose aminotransferase that has dual functions in the formation of 2-deoxy-scyllo-inosose
physiological function
-
neo6 functions as 2-deoxy-scyllo-inosose aminotransferase that has dual functions in the formation of 2-deoxy-scyllo-inosose
physiological function
the aminotransferase BtrR is involved in the biosynthesis of butirosin, a 2-deoxystreptamine-containing aminoglycoside antibiotic produced by Bacillus circulans, catalyzing the pyridoxal 5'-phosphate-dependent transamination reaction both of 2-deoxy-scylloinosose to 2-deoxy-scyllo-inosamine and of amino-dideoxy-scyllo-inosose to 2-deoxystreptamine, cf. EC 2.6.1.101
physiological function
-
the enzyme produces 2-deoxystreptamine (DOS), EC 2.6.1.101, which is the aglycone in neomycins, overview. Neo-6 is also the enzyme catalysing the transamination of 2-deoxy-scyllo-inosose, DOI, using L-glutamine as an amino donor to produce 2-deoxyscyllo-inosamine as required for 2-deoxystreptamine biosynthesis
physiological function
-
the enzyme produces 2-deoxystreptamine (DOS), EC 2.6.1.101, which is the aglycone in neomycins, overview. Neo-6 is also the enzyme catalysing the transamination of 2-deoxy-scyllo-inosose, DOI, using L-glutamine as an amino donor to produce 2-deoxyscyllo-inosamine as required for 2-deoxystreptamine biosynthesis
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physiological function
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kanB functions as 2-deoxy-scyllo-inosose aminotransferase that has dual functions in the formation of 2-deoxy-scyllo-inosose
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physiological function
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BtrR catalyzes the synthesis of 2-deoxystreptamine, which is the common aglycone of a class of aminoglycoside antibiotics, of which many are clinically important aminoglycosides like kanamycin, neomycin, gentamicin and butirosin
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additional information
active site structure of BtrR, homodimer with two active sites per dimer, BtrR with bound pyridoxamine 5'-phosphate lacks the covalent bond to Lys192. 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
additional information
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gene neo6 of the neo gene cluster and btrR from the btr gene cluster are equivalent, genetic organization, overview
additional information
the equivalent of gene neoB, from neo gene cluster, in the btr gene cluster is gene btrS
additional information
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the equivalent of gene neoB, from neo gene cluster, in the btr gene cluster is gene btrS
additional information
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gene neo6 of the neo gene cluster and btrR from the btr gene cluster are equivalent, genetic organization, overview
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additional information
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the equivalent of gene neoB, from neo gene cluster, in the btr gene cluster is gene btrS
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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
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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)
gene btrS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Escherichia coli strain JM109
gene btrS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Escherichia coli strain JM109
gene btrS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Escherichia coli strain JM109
gene btrS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression in Escherichia coli strain JM109
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Tamegai, H.; Eguchi, T.; Kakinuma, K.
First identification of Streptomyces genes involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics: genetic and evolutionary analysis of L-glutamine:2-deoxy-scyllo-inose aminotransferase genes
J. Antibiot.
55
1016-1018
2002
no activity in Streptomyces lividans, Streptomyces ribosidificus (Q4R0W2), Streptomyces fradiae (Q53U20), Streptoalloteichus hindustanus (Q6F6I1), Streptomyces kanamyceticus (Q6L739), Streptomyces ribosidificus JCM 4923 (Q4R0W2), Streptomyces kanamyceticus JCM 4433 (Q6L739), Streptomyces fradiae IFO13147 (Q53U20), Streptomyces fradiae IFO12773 (Q53U20)
brenda
Huang, F.; Haydock, S.F.; Mironenko, T.; Spiteller, D.; Li, Y.; Spencer, J.B.
The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterization of an aminotransferase involved in the formation of 2-deoxystreptamine
Org. Biomol. Chem.
3
1410-1418
2005
Streptomyces fradiae, Streptomyces fradiae NCIMB 8233
brenda
Kharel, M.K.; Subba, B.; Lee, H.C.; Liou, K.; Sohng, J.K.
Characterization of L-glutamine:2-deoxy-scyllo-inosose aminotransferase (tbmB) from Streptomyces tenebrarius
Bioorg. Med. Chem. Lett.
15
89-92
2005
Streptoalloteichus tenebrarius (Q2MF17), Streptoalloteichus tenebrarius
brenda
Kudo, F.; Yamamoto, Y.; Yokoyama, K.; Eguchi, T.; Kakinuma, K.
Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773
J. Antibiot.
58
766-774
2005
Streptomyces fradiae (Q53U20), Streptomyces fradiae, Streptomyces fradiae NBRC 12773 (Q53U20)
brenda
Jnawali, H.N.; Subba, B.; Liou, K.; Sohng, J.K.
Functional characterization of kanB by complementing in engineered Streptomyces fradiae Deltaneo6 tsr.
Biotechnol. Lett.
31
869-875
2009
Streptomyces kanamyceticus, Streptomyces, Streptomyces kanamyceticus ATCC 12853
brenda
Huang, F.; Li, Y.; Yu, J.; Spencer, J.B.
Biosynthesis of aminoglycoside antibiotics: cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine
Chem. Commun. (Camb. )
2002
2860-2861
2002
Niallia circulans (Q8G8Y2), Niallia circulans NRRL B3312 (Q8G8Y2)
brenda
Popovic, B.; Tang, X.; Chirgadze, D.Y.; Huang, F.; Blundell, T.L.; Spencer, J.B.
Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis
Proteins
65
220-230
2006
Niallia circulans (Q8G8Y2)
brenda