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Information on EC 2.6.1.101 - L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
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2.6.1.101 L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferaseIUBMB Comments
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
Reaction Schemes
Synonyms
btrR, BtrS, Gln:DOI aminotransferase, L-glutamine: 2-deoxy-scyllo-inosamine aminotransferase, L-glutamine:DOI aminotransferase, neo-6, Neo6, neoB, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
btrR
BtrS
L-glutamine:DOI aminotransferase
neo-6
Neo6
neoB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
-
-
?
additional information
?
-
NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose
2-oxoglutaramate + 2-deoxystreptamine
-
-
-
?
additional information
?
-
NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
-
-
?
additional information
?
-
NeoB also shows L-glutamine:2-deoxy-scyllo-inosose aminotransferase activity resulting in formation of 2-deoxy-scyllo-inosamine, EC 2.6.1.100
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
dependent on, binding structure and structural changes upon pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate conversion, overview
pyridoxal 5'-phosphate
the BtrR-bound pyridoxal 5'-phosphate is the essential cofactor for the amino-transfer activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene neoB, encoded in the neomycin biosynthetic gene cluster
SwissProt
brenda
gene neoB, encoded in the neomycin biosynthetic gene cluster
SwissProt
brenda
gene neo-6 encoded in the neo gene cluster
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
metabolism
evolution
additional information
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, cf. EC 2.6.1.100, and of amino-dideoxy-scyllo-inosose to 2-deoxystreptamine
physiological function
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
physiological function
-
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
-
metabolism
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
metabolism
-
the aminotransferase BtrR is involved in the biosynthesis of butirosin
metabolism
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
metabolism
-
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
-
metabolism
-
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
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evolution
BtrR and StsC are the two homologues of Neo-6 in butirosin and streptamycin biosynthetic pathways
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
evolution
-
BtrR and StsC are the two homologues of Neo-6 in butirosin and streptamycin biosynthetic pathways
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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
-
gene neo6 of the neo gene cluster and btrR from the btr gene cluster are equivalent, genetic organization, overview
additional information
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
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLADA_STRSD
Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
416
0
46095
Swiss-Prot
-
GLDSA_STRFR
424
0
44788
Swiss-Prot
Secretory Pathway (Reliability: 4)
GLDSA_STRRY
424
0
45105
Swiss-Prot
-
GLDSA_STRSD
Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
424
0
45593
Swiss-Prot
-
A0A1Y6K5W6_9CHLR
408
0
45494
TrEMBL
other Location (Reliability: 3)
A0A1D8BT93_9PSEU
424
0
45962
TrEMBL
-
A0A1J5SKD5_9ZZZZ
406
0
44119
TrEMBL
Chloroplast (Reliability: 4)
A0A149VXX5_9PROT
416
0
46228
TrEMBL
other Location (Reliability: 4)
A0A1J5QXA5_9ZZZZ
434
0
47349
TrEMBL
other Location (Reliability: 1)
A0A1J5ST00_9ZZZZ
399
0
43798
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
?
x * 46951, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE, x * 46801, recombinant His6-tagged enzyme, mass spectrometry
?
-
x * 46951, sequence calculation, x * 45000, recombinant His6-tagged enzyme, SDS-PAGE, x * 46801, recombinant His6-tagged enzyme, mass spectrometry
-
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q53U20), Streptomyces fradiae NCIMB 8233, Streptomyces fradiae NCIMB 8233 (Q53U20)
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 NBRC 12773 (Q53U20)
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
Bacillus circulans (Q8G8Y2)
brenda
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