Literature summary for 2.6.1.100 extracted from

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 (2006), Proteins, 65, 220-230.

Search for more literature for 2.6.1.100

Cloned(Commentary)

Cloned (Comment)	Organism
gene btrR, expression in Escherichia coli strain BL21 (DE3) as His-tagged enzyme	Niallia circulans

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Niallia circulans

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	no inhibition by gabaculine, i.e. 3-amino-2,3-dihydrobenzoic acid, and (amino-oxy) acetic acid	Niallia circulans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-glutamine + 2-deoxy-scyllo-inosose	Niallia circulans	-	2-oxoglutaramate + 2-deoxy-scyllo-inosamine	-	r

Organism

Organism	UniProt	Comment	Textmining
Niallia circulans	Q8G8Y2	gene btrR	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged BtrR from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration	Niallia circulans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + 2-deoxy-scyllo-inosose	-	Niallia circulans	2-oxoglutaramate + 2-deoxy-scyllo-inosamine	-	r
additional information	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	Niallia circulans	?	-	?

Subunits

Subunits	Comment	Organism
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	Niallia circulans

Synonyms

Synonyms	Comment	Organism
btrR	-	Niallia circulans

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	dependent on, binding structure and structural changes upon pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate conversion, overview	Niallia circulans

General Information

General Information	Comment	Organism
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	Niallia circulans
metabolism	the aminotransferase BtrR is involved in the biosynthesis of butirosin	Niallia circulans
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	Niallia circulans
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	Niallia circulans

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Release 2023.1 (January 2023)