Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.6.1.101 - L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase and Organism(s) Niallia circulans and UniProt Accession Q8G8Y2

for references in articles please use BRENDA:EC2.6.1.101
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Niallia circulans
UNIPROT: Q8G8Y2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Niallia circulans
The enzyme appears in selected viruses and cellular organisms
Synonyms
btrR, BtrS, Gln:DOI aminotransferase, L-glutamine: 2-deoxy-scyllo-inosamine aminotransferase, L-glutamine:DOI aminotransferase, neo-6, Neo6, neoB, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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.
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
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, binding structure and structural changes upon pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate conversion, overview
INHIBITOR
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene btrR
UniProt
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
metabolism
the aminotransferase BtrR is involved in the biosynthesis of butirosin
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLDSA_NIACI
418
0
47032
Swiss-Prot
-
SUBUNIT
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team