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Information on EC 2.3.1.29 - glycine C-acetyltransferase
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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
-
7-keto-8-aminopelargonic
-
biofs
- synthesis
The enzyme appears in viruses and cellular organisms
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, 2-amino-3-oxobutyrate coa ligase, glycine acetyltransferase, 
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SYNONYM 
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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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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KBL
2-amino-3-ketobutyrate CoA ligase
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-
-
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KBL
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enzyme is found to catalyze also the 7-keto-8-aminopelargnic acid (KAPA) synthase reaction
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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
physical interaction between threonine dehydrogenase and aminoacetone synthetase demonstrated, the two enzymes form a complex
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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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acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
-
-
-
-
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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].
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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 + aminomalonate
CoA + CO2 + 2-amino-3-oxobutanoate
-
-
same product as in reaction with glycine, aminomalonate is decarboxylated to glycine by the enzyme, in the absence of acetyl-CoA: glycine is the product
?
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
?
-
-
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
?
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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-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
specific for glycine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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succinyl-CoA
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
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not: acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: L-alanine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
no substrate: glycine methylester
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
acetyl-CoA cannot be replaced by acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
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
-
spontaneous decarboxylation to aminoacetone
?
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
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
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
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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
-
-
?
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
-
the condensation process involves the loss of the pro-R hydrogen atom of glycine and occurs with the inversion of stereochemistry
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
-
spontaneous decarboxylation to aminoacetone
r
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
-
-
spontaneous decarboxylation to aminoacetone
r
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
-
-
?
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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 + L-2-amino-3-oxobutanoate
-
condensation reaction
-
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
?
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
-
involved in L-threonine catabolism, inducible
-
-
?
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 + 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
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate is covalently bound to an active site lysine, formation of a Schiff base
pyridoxal 5'-phosphate
-
requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
-
location of pyridoxyllysine peptide in primary structure of enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phenylglyoxal
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inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
additional information
-
no inhibition by DTNB; not: PCMB, glycine methylester, glycinamide
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
by using inducible translocation trap (ITT), a reporter gene-based screening technique, nuclear translocation of 2-amino-3-ketobutyrate coenzyme A ligase (KBL) is detected in response to cold and osmotic stresses
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
2-amino-3-ketobutyrate CoA ligase of Escherichia coli is a member of the alpha-oxoamine synthase family
Show AA Sequence and Transmembrane Helices (13831 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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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
56000
84190
85000
additional information
43000
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
additional information
-
when loaded together threonine dehydrogease and aminoacetone synthetase co-eludes at a molecular weight of 150000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 43117.15, recombinant enzyme, mass spectrometry, x * 43000, recombinant enzyme, SDS-PAGE
dimer
monomer
additional information
-
the threonine dehydrogenase and the aminoacetone synthetase form a complex with an apparent stoichiometry of two dimers of aminoacetone synthetase to one threonine dehydrogenase tetramer
dimer
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
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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
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