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EC Tree
IUBMB Comments This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine . This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex .
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aminoacetone synthetase, 2-amino-3-ketobutyrate coa ligase, 2-amino-3-ketobutyrate coenzyme a ligase, aminoacetone synthase, 2-amino-3-ketobutyrate-coa ligase, glycine c-acetyltransferase, glycine acetyltransferase, 2-amino-3-oxobutyrate coa ligase,
more
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2-amino-3-ketobutyrate CoA ligase
2-amino-3-ketobutyrate coenzyme A ligase
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2-amino-3-ketobutyrate-CoA ligase
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2-amino-3-oxobutyrate CoA ligase
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acetyltransferase, glycine
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alpha-amino-beta-oxobutyrate CoA-ligase
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aminoacetone synthase
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aminoacetone synthetase
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glycine acetyltransferase
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2-amino-3-ketobutyrate CoA ligase
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2-amino-3-ketobutyrate CoA ligase
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acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
reaction mechanism
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
the condensation process involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry
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Acyl group transfer
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acetyl-CoA:glycine C-acetyltransferase
This is a pyridoxal-phosphate-dependent enzyme that acts in concert with EC 1.1.1.103, L-threonine 3-dehydrogenase, in the degradation of threonine to form glycine [3]. This threonine degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [4].
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
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condensation reaction
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?
n-butyryl-CoA + glycine
CoA + 2-amino-3-oxohexanoate
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reaction at 16% the rate of acetyl-CoA
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?
n-propionyl-CoA + glycine
CoA + 2-amino-3-oxopentanoate
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reaction at 127% the rate of acetyl-CoA
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?
additional information
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the enzyme catalyzes the exchange of pro-R hydrogen of glycine with protons in the medium
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?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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spontaneous decarboxylation to aminoacetone
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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not: valeryl-CoA, glutaryl-CoA
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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specific for glycine
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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specific for glycine
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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succinyl-CoA
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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no substrate: L-alanine
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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no substrates: glycinamide, 2-aminoethanol, aminomethylphosphonic acid, aminomalonate
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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no substrate: glycine methylester
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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no substrates: L-serine, L-threonine, L-valine, L-leucine
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r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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involved in L-threonine catabolism, inducible
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?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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the condensation process involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry
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?
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
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acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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involved in L-threonine catabolism, inducible
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acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
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condensation reaction
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
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location of pyridoxyllysine peptide in primary structure of enzyme
pyridoxal 5'-phosphate
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active-site mapping
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1,2-Cyclohexanedione
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inactivation
2,3-Butanedione
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inactivation
4-(Oxoacetyl)phenoxyacetic acid
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Aminomethylphosphonic acid
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hydroxylamine
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pyridoxal 5'-phosphate restores
Phenylglyoxal
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inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
additional information
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no inhibition by DTNB
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additional information
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not: PCMB, glycine methylester, glycinamide
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5,5'-dithiobis(2-nitrobenzoic acid)
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additional information
additional information
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kinetics of the exchange of pro-R hydrogen of glycine with protons in the medium by the enzyme
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0.14
aminomalonic acid
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3.6
Aminomethylphosphonic acid
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6 - 9
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about 30% of maximal activity at pH 6.0 and 43% at 9.0
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SwissProt
brenda
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evolution
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2-amino-3-ketobutyrate CoA ligase of Escherichia coli is a member of the alpha-oxoamine synthase family
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43000
2 * 43000, SDS-PAGE
80000
dynamic ligth scattering measurement
41690
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2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
41930
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2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
42093
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2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
43000
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x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
90480
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sucrose density gradient centrifugation
additional information
nucleotide sequence
84190
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84190
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calculated from amino acid composition
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dimer
2 * 43000, SDS-PAGE
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x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
dimer
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dimer
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2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
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side-chain modification
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the phenylglyoxal-inactivated enzyme is associated with the loss of 1.5 arginine residue per ligase subunit
additional information
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no carbohydrates
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external aldimine in the crystal structure, interaction between aldimine and the side chains in the substrate binding site explain the specificity to the substrate
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ethylene glycol, 20%, stabilizes
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glycerol, 10% v/v, stabilizes
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recombinant enzyme by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration
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expressed in Escherichia coli
recombinant expresssion in Escherichia coli
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Mukherjee, J.J.; Dekker, E.E.
Purification, properties, and N-terminal amino acid sequence of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA ligase, a pyridoxal phosphate-dependent enzyme
J. Biol. Chem.
262
14441-14447
1987
Escherichia coli
brenda
Mukherjee, J.J.; Dekker, E.E.
Inactivation of Escherichia coli 2-amino-3-ketobutyrate CoA ligase by phenylglyoxal and identification of an active-site arginine peptide
Arch. Biochem. Biophys.
299
147-153
1992
Escherichia coli
brenda
Mukherjee, J.J.; Dekker, E.E.
2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: stoichiometry of pyridoxal phosphate binding and location of the pyridoxyllysine peptide in the primary structure of the enzyme
Biochim. Biophys. Acta
1037
24-29
1990
Escherichia coli
brenda
Aronson, B.D.; Ravnikar, P.D.; Somerville, R.L.
Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) gene of E. coli
Nucleic Acids Res.
16
3586
1988
Escherichia coli (P0AB77)
brenda
Edgar, A.J.; Polak, J.M.
Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs
Eur. J. Biochem.
267
1805-1812
2000
Bos taurus, Escherichia coli (P0AB77), Escherichia coli, Homo sapiens, Mus musculus
brenda
Bashir, Q.; Rashid, N.; Akhtar, M.
Mechanism and substrate stereochemistry of 2-amino-3-oxobutyrate CoA ligase: implications for 5-aminolevulinate synthase and related enzymes
Chem. Commun. (Camb. )
2006
5065-5067
2006
Escherichia coli
brenda
Jamil, F.
Kinetics of the exchange reaction catalyzed by 2-amino-3-ketobutyrate CoA ligase
Front. Biol.
10
503-507
2015
Escherichia coli
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brenda