Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
the enzyme shows a catalytic reaction mechanism that proceeds through deprotonation of the 3-keto-5-aminohexanoate substrate, nucleophilic addition onto an incoming acetyl-CoA, intramolecular transfer of the CoA moiety, and final retro-Claisen reaction leading to acetoacetate and 3-aminobutyryl-CoA, structure-function analysis, docking study and molecular modeling, detailed overview. Absence of detection of any covalent acyl-enzyme intermediate
Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
dependent on, one metal ion per subunit and active site, coordinated by His46, His48, and Glu230 in the active site. The metal ion is situated at the bottom of a crevice accessible from two opposite openings, one of which is delimited by the mobile beta3-alpha3 loop
enzyme structure determination and analysis, the active site is situated in each monomer at the C-terminal face of the central beta-barrel with a metal ion coordinated by His46, His48, and Glu230, overview
the enzyme is a representative of a large family of prokaryotic hypothetical proteins, annotated as the domain of unknown function DUF849, it shows the ubiquitous triose phosphate isomerase (TIM) barrel fold and a Zn2+ cation reminiscent of metal-dependent class II aldolases
the enzyme is involved in the the 3-keto-5-aminohexanoate pathway of lysine degradation, tracer experiments on acetate and butyrate formation from lysine and acetate, overview
C-1 and C-2 of 3-oxo-5-aminohexanoate are converted mainly to acetoacetate and acetate, whereas C-3 to C-6 are converted mainly to 3-hydroxybutyrate or its coenzyme A thiolester. 3-Aminobutyryl-CoA is then deaminated to form crotonyl-CoA. The enzymes observed in extracts of Brevibacterium sp. can account for the conversion of 3,5-diaminohexanoate to acetyl-CoA, overview
C-1 and C-2 of 3-oxo-5-aminohexanoate are converted mainly to acetoacetate and acetate, whereas C-3 to C-6 are converted mainly to 3-hydroxybutyrate or its coenzyme A thiolester. 3-Aminobutyryl-CoA is then deaminated to form crotonyl-CoA. The enzymes observed in extracts of Brevibacterium sp. can account for the conversion of 3,5-diaminohexanoate to acetyl-CoA, overview
the enzyme is involved in the fermentation pathway of lysine; the enzyme is involved in the the 3-keto-5-aminohexanoate pathway of lysine degradation, tracer experiments on acetate and butyrate formation from lysine and acetate, overview
each subunit of 276 residues shows the canonical (beta/alpha)8 TIM barrel fold, with a short additional C-terminal alpha-helix (alpa9) protruding at the N-terminal face of the barrel and three beta-turn extensions coming out from the barrel core, inserted in between beta2 and alpha2 (residues 49-58), beta4 and alpha4 (residues 112-119), and beta8 and alpha8 (residues 234-240)
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
native state enzyme, as well as enzyme complexed with substrate (5S)-5-amino-3-oxohexanoate or product acetoacetate, X-ray diffraction structure determination and analysis at 1.28-1.84 A resolution, molecular replacement
native soluble enzyme 78fold by ammonium sulfate fractionation and anion exchange chromatography, followed by ultrafiltration and adsorption chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, desalting gel filtration, anion exchange chromatography, and gel filtration
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene kce, DNA and amino acid sequence determination and analysis, genetic structure and comparison, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 DE3
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2.3.1.247 3-keto-5-aminohexanoate cleavage enzyme
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