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Information on EC 2.3.1.29 - glycine C-acetyltransferase and Organism(s) Escherichia coli and UniProt Accession P0AB77
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2.3.1.29 glycine C-acetyltransferaseIUBMB 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 .
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Word Map
- 2.3.1.29
- l-threonine
- pyridoxal
- 5'-phosphate
- 5-aminolevulinate
-
1.1.1.103
- 8-amino-7-oxononanoate
-
5'-phosphate-dependent
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7-keto-8-aminopelargonic
-
biofs
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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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-
-
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acetyltransferase, glycine
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-
-
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alpha-amino-beta-oxobutyrate CoA-ligase
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-
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aminoacetone synthase
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-
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aminoacetone synthetase
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-
-
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glycine acetyltransferase
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-
-
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2-amino-3-ketobutyrate CoA ligase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-
SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY
37257-11-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
-
condensation reaction
-
-
?
n-butyryl-CoA + glycine
CoA + 2-amino-3-oxohexanoate
-
reaction at 16% the rate of acetyl-CoA
-
-
?
n-propionyl-CoA + glycine
CoA + 2-amino-3-oxopentanoate
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reaction at 127% the rate of acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme catalyzes the exchange of pro-R hydrogen of glycine with protons in the medium
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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spontaneous decarboxylation to aminoacetone
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
not: valeryl-CoA, glutaryl-CoA
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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specific for glycine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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specific for glycine
-
-
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
-
-
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
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + 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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
-
condensation reaction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
location of pyridoxyllysine peptide in primary structure of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phenylglyoxal
-
inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of the exchange of pro-R hydrogen of glycine with protons in the medium by the enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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2-amino-3-ketobutyrate CoA ligase of Escherichia coli is a member of the alpha-oxoamine synthase family
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41690
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
41930
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
42093
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
43000
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
84190
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
dimer
dimer
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
the phenylglyoxal-inactivated enzyme is associated with the loss of 1.5 arginine residue per ligase subunit
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
external aldimine in the crystal structure, interaction between aldimine and the side chains in the substrate binding site explain the specificity to the substrate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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)
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
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
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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