Information on EC 2.3.1.29 - glycine C-acetyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.29
-
RECOMMENDED NAME
GeneOntology No.
glycine C-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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-
L-threonine degradation II
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threonine metabolism
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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 hide
37257-11-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
grown on L-threonine
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + aminomalonate
CoA + CO2 + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
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
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
acetyl-CoA + glycine
CoA + L-2-amino-3-oxobutanoate
show the reaction diagram
-
-
-
-
?
acetyl-CoA + L-alanine
CoA + ?
show the reaction diagram
-
-
-
-
?
n-butyryl-CoA + glycine
CoA + 2-amino-3-oxohexanoate
show the reaction diagram
-
reaction at 16% the rate of acetyl-CoA
-
-
-
n-propionyl-CoA + glycine
CoA + 2-amino-3-oxopentanoate
show the reaction diagram
-
reaction at 127% the rate of acetyl-CoA
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-
-
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
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Cyclohexanedione
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inactivation
2,3-Butanedione
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inactivation
4-(Oxoacetyl)phenoxyacetic acid
-
-
aminomalonic acid
-
-
Aminomethylphosphonic acid
-
-
Aminooxyacetate
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-
Cd2+
-
strong
Cu2+
-
strong
glutathione
Glycine methyl ester
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inactivation
Hg2+
-
strong
hydroxylamine
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pyridoxal 5'-phosphate restores
L-cysteine
Phenylglyoxal
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inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
phenylhydrazine
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-
Semicarbazide
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-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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-
iodoacetamide
N-ethylmaleimide
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p-mercuribenzoate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.059
acetyl-CoA
12
Butyryl-CoA
-
-
0.25 - 22
glycine
11.8
L-alanine
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-
0.08
propionyl-CoA
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
aminomalonic acid
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-
3.6
Aminomethylphosphonic acid
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16.4
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-
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pI: 5.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 9.4
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absorbtion spectrum does not change significantly
6 - 9
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about 30% of maximal activity at pH 6.0 and 43% at 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
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-
58330
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calculated from amino acid composition
80000
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dynamic ligth scattering measurement
90480
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sucrose density gradient centrifugation
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
no carbohydrates
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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stable
486744
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme shows high thermostability at 70°C for 1 h and a half-life of 1 h at 80°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA, 1 mM, stabilizes
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ethylene glycol, 20%, stabilizes
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glycerol, 10% v/v, stabilizes
glycine stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bovine partial; expressed in Escherichia coli
overexpressed in Escherichia coli
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