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EC Tree
IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
l-threonine aldolase, l-threonine acetaldehyde-lyase,
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L-threonine acetaldehyde-lyase
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L-TA
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L-threonine aldolase
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L-threonine aldolase
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L-threonine = glycine + acetaldehyde
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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.
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alpha-methyl-beta-phenylserine
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D-alanine + 3-nitrobenzaldehyde
beta-(3-nitrophenyl)-alpha-methyl-serine
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23% conversion
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?
D-alanine + benzaldehyde
2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid
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10% conversion
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D-alanine + hexanal
2-amino-3-hydroxy-2-methyloctanoic acid
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4% conversion
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D-beta-phenylserine
glycine + benzaldehyde
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D-serine + 3-nitrobenzaldehyde
beta-(3-nitrophenyl)-alpha-hydroxymethyl-serine
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2% conversion
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D-serine + benzaldehyde
2-amino-3-hydroxy-2-hydroxymethyl-3-phenylpropanoic acid
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4% conversion
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D-threonine
glycine + acetaldehyde
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glycine + acetaldehyde
L-threonine
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r
L-threonine
glycine + acetaldehyde
L-allo-threonine
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L-allo-threonine
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L-allo-threonine
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L-threonine
glycine + acetaldehyde
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L-TA preferably accepts L-threonine as substrate
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L-threonine
glycine + acetaldehyde
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no activity with L-allo-threonine
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L-threonine
glycine + acetaldehyde
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the enzyme is highly specific for L-threonine, no activity with D-threonine, no activity with DL-allo-threonine
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r
L-threonine
glycine + acetaldehyde
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L-TA preferably accepts L-threonine as substrate
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?
L-threonine
glycine + acetaldehyde
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r
L-threonine
glycine + acetaldehyde
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L-TA preferably accepts L-threonine as substrate
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?
L-threonine
glycine + acetaldehyde
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L-TA preferably accepts L-threonine as substrate
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?
L-threonine
glycine + acetaldehyde
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L-TA preferably accepts L-threonine as substrate
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?
L-threonine
glycine + acetaldehyde
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r
L-threonine
glycine + acetaldehyde
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r
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
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dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate-dependent enzyme
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additional information
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no requirement for metal ions
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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
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
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
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Starvation
[Effects of starvation, a hyperprotein diet and treatment with nicotinamide on L-threonine aldolase and allothreonine aldolase in the rat liver]
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2.76
alpha-methyl-beta-phenylserine
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25°C, pH 8.0
2
D-beta-phenylserine
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25°C, pH 8.0
10.9
D-threonine
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pH 8.0, temperature not specified in the publication
0.19 - 14.6
L-allo-threonine
0.19
L-allo-threonine
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pH and temperature not specified in the publication
14.6
L-allo-threonine
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pH and temperature not specified in the publication
0.42
L-threonine
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pH 7.0, 30°C
10
L-threonine
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pH and temperature not specified in the publication
14.7
L-threonine
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pH and temperature not specified in the publication
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0.54
alpha-methyl-beta-phenylserine
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25°C, pH 8.0
18.3
D-beta-phenylserine
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25°C, pH 8.0
0.2
D-threonine
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pH 8.0, temperature not specified in the publication
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0.195
alpha-methyl-beta-phenylserine
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25°C, pH 8.0
9.2
D-beta-phenylserine
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25°C, pH 8.0
0.0027
D-threonine
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pH 8.0, temperature not specified in the publication
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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
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additional information
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the crude extract has a specific activity of 0.02 units/mg, the purified enzyme has a specific activity of 0.32 units/mg, pH and temperature not specified in the publication
additional information
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specific activity of 31 units/mg, using L-threonine as substrate, pH and temperature not specified in the publication
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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
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tetramer
4 * 37000, SDS-PAGE
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A21C
L-threonine cleavage activity is similar to the activity of the wild-type enzyme
F85Y
L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme
I124D
L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme
P56C
L-threonine cleavage activity is about 95% of the activity of the wild-type enzyme, the mutant enzyme displays significantly enhanced stability compared to the wild type enzyme
Q22K
L-threonine cleavage activity is about 75% of the activity of the wild-type enzyme
S198D
L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme
T59D
L-threonine cleavage activity is about 10% of the activity of the wild-type enzyme
V235C
L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme
V29D
L-threonine cleavage activity is about 90% of the activity of the wild-type enzyme
W86E
the mutant enzyme displays enhanced activity, with stability similar to the wild type enzyme
additional information
rational design is applied to the enzyme to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer
additional information
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rational design is applied to the enzyme to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer
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75
15 h, 50% loss of activity
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0-5°C, activity slowly decreases to 50% of the original activity after 10 days
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DEAE-cellulose column chromatography
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DEAE-Toyopearl column chromatography
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overexpression in Escherichia coli
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the gene of L-threonine aldolase from Thermotoga maritima is cloned into c-LEctas expression vector pLE1A17 under control of the T7 promoter. Expression in Escherichia coli BL21(DE3)
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biotechnology
development of a growth-dependent selection system for identification of L-threonine aldolases in Pseudomonas putida KT2440. The functionality is demonstrated with different growth studies by introducing recombinant, nonnative The functionality was demonstrated with different growth studies by introducing recombinant, nonnative threonine aldolases into the selection strain, restoring its deficiency in growth in minimal medium supplemented with DL-threo-beta-phenylserine as sole carbon source
synthesis
threonine aldolase is a very promising enzyme that can be used to prepare biologically active compounds or building blocks for pharmaceutical industry. Rational design is applied to thermophilic threonine aldolase from Thermotoga maritima to improve thermal stability by the incorporation of salt and disulfide bridges between subunits in the functional tetramer
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Stoecklein, W.; Schmidt, H.L.
Evidence for L-threonine cleavage and allo-threonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase
Biochem. J.
232
621-622
1985
Clostridium pasteurianum
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Dainty, R.H.
Purification and properties of threonine aldolase from Clostridium pasteurianum
Biochem. J.
117
585-592
1970
Clostridium pasteurianum
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Riario-Sforza, G.; Pagani, R.; Marinello, E.
Threonine aldolase and allothreonine aldolase in rat liver
Eur. J. Biochem.
8
88-92
1969
Rattus norvegicus
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Pagani, R.; Leoncini, R.; Terzuoli, L.; John, C.; Pizzichini, M.; Marinello, E.
DL-Allothreonine and L-threonine aldolase in rat liver
Biochem. Soc. Trans.
19
346S
1991
Rattus norvegicus
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Dueckers, N.; Baer, K.; Simon, S.; Groeger, H.; Hummel, W.
Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids
Appl. Microbiol. Biotechnol.
88
409-424
2010
Clostridium pasteurianum, Escherichia coli, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas sp. NCIMB10558
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Karasek, M.A.
Greenberg, D.M.: Studies on the properties of threonine aldolases
J. Biol. Chem.
227
191-205
1957
Ovis aries
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Bulut, D.; Grger, H.; Hummel, W.
Development of a growth-dependent selection system for identification of L-threonine aldolases
Appl. Microbiol. Biotechnol.
99
5875-5883
2015
Pseudomonas putida (Q88R13)
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Fesko, K.; Strohmeier, G.A.; Breinbauer, R.
Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary alpha-amino acids
Appl. Microbiol. Biotechnol.
99
9651-9661
2015
Aeromonas veronii
brenda
Wieteska, L.; Ionov, M.; Szemraj, J.; Feller, C.; Kolinski, A.; Gront, D.
Improving thermal stability of thermophilic L-threonine aldolase from Thermotoga maritima
J. Biotechnol.
199
69-76
2015
Thermotoga maritima (Q9X266), Thermotoga maritima
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