Information on EC 4.1.2.5 - L-threonine aldolase

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

EC NUMBER
COMMENTARY hide
4.1.2.5
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RECOMMENDED NAME
GeneOntology No.
L-threonine aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-threonine = glycine + acetaldehyde
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycine biosynthesis IV
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Glycine, serine and threonine metabolism
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L-threonine degradation IV
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threonine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-threonine acetaldehyde-lyase (glycine-forming)
A pyridoxal-phosphate protein. This enzyme is specific for L-threonine and can not utilize L-allo-threonine. Different from EC 4.1.2.49, L-allo-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Pseudomonas sp. NCIMB10558
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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
L-allo-threonine
?
show the reaction diagram
L-threonine
glycine + acetaldehyde
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no requirement for metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate
acetaldehyde
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the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition
Cu2+
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cysteine
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activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate
glycine
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the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition
Hg2+
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hydroxylamine
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1 mM, complete inhibition
p-chloromercuribenzoate
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0.01 mM, complete inhibition
Semicarbazide
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1 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 14.6
L-allo-threonine
0.42 - 14.7
L-threonine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
acetaldehyde
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pH and temperature not specified in the publication
0.01
glycine
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.8
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pH 6.0: about 80% of maximal activity, pH 7.8: about 80% of maximal activity
6.5 - 8
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pH 6.5: about 60% of maximal activity, pH 8.0: about 40% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-5°C, activity slowly decreases to 50% of the original activity after 10 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography
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DEAE-Toyopearl column chromatography
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