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.
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The enzyme appears in viruses and cellular organisms
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.
BtrR accepts four different carbocyclic substrates, 2-deoxy-scyllo-inosose, 2-deoxy-scyllo-inosamine, amino-dideoxyscyllo-inosose, and 2-deoxysteptamine, requiring the binding site in the enzyme to have some flexibility. NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
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, cf. EC 2.6.1.100, and of amino-dideoxy-scyllo-inosose to 2-deoxystreptamine
the enzyme produces 2-deoxystreptamine (DOS), 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, function of Neo-6 as the L-glutamine:DOI aminotransferase
the enzyme produces 2-deoxystreptamine (DOS), 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, function of Neo-6 as the L-glutamine:DOI aminotransferase
purified Neo-6 also catalyses the amino transfer from L-glutamine to 2-deoxyscyllo-inosose to produce 2-deoxyscyllo-inosamine when coupled with BtrC in the presence of G6P, NAD+, Co2+ and L-glutamine, EC 2.6.1.100
the enzyme is involved in the biosynthesis of the 2-deoxystreptamine (DOS)-containing aminoglycoside neomycin. 3-Amino-2,3-dideoxy-scyllo-inosose produced by the NeoA reaction is continuously used as substrate for the natural forward transamination catalyzed by NeoB in the 2-deoxystreptamine biosynthesis. NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
purified Neo-6 also catalyses the amino transfer from L-glutamine to 2-deoxyscyllo-inosose to produce 2-deoxyscyllo-inosamine when coupled with BtrC in the presence of G6P, NAD+, Co2+ and L-glutamine, EC 2.6.1.100
the enzyme is involved in the biosynthesis of the 2-deoxystreptamine (DOS)-containing aminoglycoside neomycin. 3-Amino-2,3-dideoxy-scyllo-inosose produced by the NeoA reaction is continuously used as substrate for the natural forward transamination catalyzed by NeoB in the 2-deoxystreptamine biosynthesis. NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
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
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
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
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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
The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterization of an aminotransferase involved in the formation of 2-deoxystreptamine