Information on EC 2.3.1.29 - glycine C-acetyltransferase

New: Word Map on EC 2.3.1.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
2.3.1.29
-
RECOMMENDED NAME
GeneOntology No.
glycine C-acetyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
show the reaction diagram
physical interaction between threonine dehydrogenase and aminoacetone synthetase demonstrated, the two enzymes form a complex; reaction mechanism
-
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
show the reaction diagram
reaction mechanism
-
acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate
show the reaction diagram
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 + L-2-amino-3-oxobutanoate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-threonine degradation II
-
-
threonine metabolism
-
-
Glycine, serine and threonine metabolism
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-amino-3-ketobutyrate CoA ligase
-
-
-
-
2-amino-3-ketobutyrate coenzyme A ligase
-
-
-
-
2-amino-3-ketobutyrate-CoA ligase
-
-
-
-
2-amino-3-oxobutyrate CoA ligase
-
-
acetyltransferase, glycine
-
-
-
-
alpha-amino-beta-oxobutyrate CoA-ligase
-
-
-
-
aminoacetone synthase
-
-
-
-
aminoacetone synthetase
-
-
-
-
glycine acetyltransferase
-
-
-
-
KBL
-
enzyme is found to catalyze also the 7-keto-8-aminopelargnic acid (KAPA) synthase reaction
CAS REGISTRY NUMBER
COMMENTARY
37257-11-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
grown on L-threonine
-
-
Manually annotated by BRENDA team
K-12-mutant SBD-76, grown on L-threonine
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
spontaneous decarboxylation to aminoacetone
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
-
spontaneous decarboxylation to aminoacetone
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
not: valeryl-CoA, glutaryl-CoA
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
specific for glycine
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
specific for glycine
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
specific for glycine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
succinyl-CoA
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
succinyl-CoA, not: acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
no substrate: L-alanine
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
no substrate: L-alanine
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
no substrates: glycinamide, 2-aminoethanol, aminomethylphosphonic acid, aminomalonate, no substrate: glycine methylester
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
no substrate: glycine methylester
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
no substrates: L-serine, L-threonine, L-valine, L-leucine
-
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
acetyl-CoA cannot be replaced by acetyl phosphate
spontaneous decarboxylation to aminoacetone
r
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
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 + 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
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
involved in L-threonine catabolism, inducible
-
-
acetyl-CoA + glycine
CoA + 2-amino-3-oxobutanoate
show the reaction diagram
-
enzyme catalyzes the second reaction step on the main metabolic degradation pathway for threonine
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
active-site mapping
pyridoxal 5'-phosphate
-
location of pyridoxyllysine peptide in primary structure of enzyme; requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
-
requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate is covalently bound to an active site lysine, formation of a Schiff base; requirement, stoichiometry: 1 mol per mol subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-Cyclohexanedione
-
inactivation
2,3-Butanedione
-
inactivation
4-(Oxoacetyl)phenoxyacetic acid
-
-
aminomalonic acid
-
-
Aminomethylphosphonic acid
-
-
Aminooxyacetate
-
-
Cd2+
-
strong
CoA
-
strong
Cu2+
-
strong
glutathione
-
-
glutathione
-
-
Glycine methyl ester
-
inactivation
Hg2+
-
strong
hydroxylamine
-
pyridoxal 5'-phosphate restores
IAA
-
-
L-cysteine
-
-
L-cysteine
-
-
L-cysteine
-
enzyme reacts reversibly with L-cysteine
Phenylglyoxal
-
inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
phenylhydrazine
-
-
Semicarbazide
-
-
additional information
-
no inhibition by DTNB; not: glycine
-
additional information
-
no inhibition by DTNB; not: PCMB, glycine methylester, glycinamide
-
additional information
-
no inhibition by DTNB
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
iodoacetamide
-
increases yield of aminoacetone by 50%
iodoacetamide
-
not
N-ethylmaleimide
-
-
p-mercuribenzoate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
acetyl-CoA
-
-
0.053
acetyl-CoA
-
-
0.059
acetyl-CoA
-
-
12
Butyryl-CoA
-
-
0.25
glycine
-
-
12
glycine
-
-
22
glycine
-
-
11.8
L-alanine
-
-
0.08
propionyl-CoA
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
aminomalonic acid
-
-
3.6
Aminomethylphosphonic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16.4
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
-
additional information
-
pI: 5.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 9.4
-
absorbtion spectrum does not change significantly
6 - 9
-
about 30% of maximal activity at pH 6.0 and 43% at 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme synthesized in cytoplasm
Manually annotated by BRENDA team
-
KBL is localised in the cytoplasm of NIH3T3 cells
Manually annotated by BRENDA team
-
enzyme imported into mitochondrion from cytoplasm
Manually annotated by BRENDA team
-
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
LITERATURE
43000
-
-
486746
43000
-
SDS-PAGE
685670
44000
-
-
486745
56000
-
gel filtration
285713
56000
-
gel filtration
486744
58330
-
calculated from amino acid composition
486744
80000
-
dynamic ligth scattering measurement
486747
84190
-
calculated from amino acid composition
486740
84190
-
-
486742
85000
-
gel filtration
486740
85000
-
native PAGE
685670
90480
-
sucrose density gradient centrifugation
486740
additional information
-
when loaded together threonine dehydrogease and aminoacetone synthetase co-eludes at a molecular weight of 150000 Da
285713
additional information
-
nucleotide sequence
486743
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 41690, gel filtration, denaturating conditions, 2 * 41930, SDS-PAGE, 2 * 42093, calculated from amino acid composition
dimer
-
2 * 28000, SDS-PAGE, 2 * 29165, calculated from amino acid composition
dimer
-
-
dimer
-
2 * 43000, SDS-PAGE
dimer
-
native PAGE
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
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
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
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
stable
486744
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme shows high thermostability at 70°C for 1 h and a half-life of 1 h at 80°C
685670
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 10% v/v, stabilizes
-
glycine stabilizes
-
EDTA, 1 mM, stabilizes
-
ethylene glycol, 20%, stabilizes
-
glycerol, 10% v/v, stabilizes
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bovine partial; expressed in Escherichia coli
-
overexpressed in Escherichia coli
-