Information on EC 2.3.1.247 - 3-keto-5-aminohexanoate cleavage enzyme

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.247
-
RECOMMENDED NAME
GeneOntology No.
3-keto-5-aminohexanoate cleavage enzyme
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(5S)-5-amino-3-oxohexanoate + acetyl-CoA = L-3-aminobutanoyl-CoA + acetoacetate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Claisen condensation
uncommon Claisen-type condensation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine fermentation to acetate and butanoate
-
-
Lysine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase
Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
additional information
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5S)-5-amino-3-oxohexanoate + acetyl-CoA
L-3-aminobutanoyl-CoA + acetoacetate
show the reaction diagram
beta-alanyl-CoA + acetoacetate
?
show the reaction diagram
DL-3-aminobutanoyl-CoA + 2-methylacetoacetate
(5S)-5-amino-2-methyl-3-oxohexanoate + acetyl-CoA
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5S)-5-amino-3-oxohexanoate + acetyl-CoA
L-3-aminobutanoyl-CoA + acetoacetate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
strong activation
Mn2+
moderate activation
Zn2+
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
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
activates at low concentrations in the presence of a higher concentration of CoCl2, inhibits at 0.1-1.0 mM by 30%
phosphate
-
weak inhibition
potassium phosphate
4, 15, 30, 65, and 85% inhibition at 0.2, 0.4, 1.0, 10, and 100 mM, respectively
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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EDTA
activates at low concentrations in the presence of a higher concentration of CoCl2, inhibits at 0.1-1.0 mM by 30%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.208 - 1.181
(5S)-5-amino-3-oxohexanoate
-
0.012 - 0.046
acetyl-CoA
additional information
additional information
steady-state kinetic analysis of wild-type and mutant enzymes, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 2.69
(5S)-5-amino-3-oxohexanoate
-
0.32 - 2.69
acetyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 12.9
(5S)-5-amino-3-oxohexanoate
202563
2.8 - 224.2
acetyl-CoA
29
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.105
-
crude enzyme extract, pH 7.0, 25C
0.18
curde enzyme extract, pH 7.0, 25C
12.5
-
purified enzyme, pH 7.0, 25C
15.7
purified enzyme, pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
forward reaction
7
-
forward reaction assay at
8
-
reverse reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.1
50% of maximal activity at pH 5.2 and pH 8.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Cloacimonas acidaminovorans (strain Evry)
Cloacimonas acidaminovorans (strain Evry)
Cloacimonas acidaminovorans (strain Evry)
Cloacimonas acidaminovorans (strain Evry)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
about, gel filtration
123000
-
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 143fold by anion exchange chromatography
native soluble enzyme 78fold by ammonium sulfate fractionation and anion exchange chromatography, followed by ultrafiltration and adsorption chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, desalting gel filtration, anion exchange chromatography, and gel filtration
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D231G
site-directed mutagenesis, inactive mutant
E143G
site-directed mutagenesis
E143Q
site-directed mutagenesis
R226G
site-directed mutagenesis, inactive mutant
S82G
site-directed mutagenesis