Information on EC 4.1.2.49 - L-allo-threonine aldolase

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The expected taxonomic range for this enzyme is: Aeromonas jandaei

EC NUMBER
COMMENTARY hide
4.1.2.49
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RECOMMENDED NAME
GeneOntology No.
L-allo-threonine aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-allo-threonine = glycine + acetaldehyde
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-allo-threonine acetaldehyde-lyase (glycine-forming)
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DL-beta-hydroxynorvaline + H2O
glycine + propionaldehyde
show the reaction diagram
DL-threo-3,4-dihydroxyphenylserine + H2O
glycine + 3,4-dihydroxybenzaldehyde
show the reaction diagram
DL-threo-beta-phenylserine + H2O
glycine + benzaldehyde
show the reaction diagram
Vmax/KM is 33% compared to DL-threo-3,4-dihydroxyphenylserine
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?
L-allo-threonine
glycine + acetaldehyde
show the reaction diagram
additional information
?
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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
L-allo-threonine
glycine + acetaldehyde
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
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1 mM, 76% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
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1 mM, 100% inhibition
Acriflavine
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1 mM, 65% inhibition
Ag2SO4
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1 mM, 100% inhibition
AlCl3
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1 mM, 69% inhibition
CdCl2
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1 mM, 80% inhibition
D-(-)-penicillamine
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1 mM, 87% inhibition
FeCl3
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1 mM, 100% inhibition
FeSO4
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1 mM, 100% inhibition
HgCl2
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1 mM, 99% inhibition
hydroxylamine
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1 mM, 100% inhibition
iodoacetamide
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1 mM, 56% inhibition
N-bromosuccinimide
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1 mM, 89% inhibition
phenylhydrazine
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1 mM, 91% inhibition
Semicarbazide
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1 mM, 63% inhibition
ZnSO4
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1 mM, 98% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.8
DL-beta-hydroxynorvaline
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pH 7.4, temperature not specified in the publication
6.77
DL-threo-3,4-Dihydroxyphenylserine
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pH 7.4, temperature not specified in the publication
19.6
DL-threo-beta-phenylserine
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pH 7.4, temperature not specified in the publication
0.36 - 1.45
L-allo-threonine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 3
L-allo-threonine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.9 - 8.1
L-allo-threonine
2967
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
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pH 8.0, 30°C
37.1
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DL-beta-hydroxynorvaline, pH 7.4, temperature not specified in the publication
45.2
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L-allo-threonine, pH 7.4, temperature not specified in the publication
208
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DL-threo-beta-phenylserine, pH 7.4, temperature not specified in the publication
217
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DL-threo-3,4-dihydroxyphenylserine, pH 7.4, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36294
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4 * 36294, calculated from sequence
38000
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4 * 38000, SDS-PAGE
160000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in recombinant Escherichia coli cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K199A
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catalytically inactive mutant enzyme
K224A
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mutant enzyme shows properties similar to the wild type enzyme
K51A
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mutant enzyme shows properties similar to the wild type enzyme
K199A
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catalytically inactive mutant enzyme
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K224A
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mutant enzyme shows properties similar to the wild type enzyme
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K51A
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mutant enzyme shows properties similar to the wild type enzyme
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