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Information on EC 4.1.2.42 - D-threonine aldolase
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4.1.2.42 D-threonine aldolaseIUBMB Comments
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine . Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate .
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Word Map
- 4.1.2.42
- synthesis
- arthrobacter
- 5'-phosphate
- alcaligenes
-
d-specific
-
low-specificity
- pharmacology
- xylosoxidans
-
chlamydomonas
- medicine
-
alpha-position
-
plp-dependent
- reinhardtii
- l-threonine
- dehydratase
-
beta-position
-
pyridoxal-p
- aldolases
-
erythro
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
ARDTA, AXDTA, CrDTA, D-TA, D-threonine aldolase, DTA, low specificity D-TA, low specificity D-threonine aldolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ARDTA
AXDTA
D-threonine aldolase
DTA
low specificity D-TA
low specificity D-threonine aldolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-allothreonine = glycine + acetaldehyde
-
-
-
-
D-threonine = glycine + acetaldehyde
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
D-threonine acetaldehyde-lyase (glycine-forming)
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine [1]. Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate [1].
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CAS REGISTRY NUMBER
COMMENTARY
87588-22-5
-
9024-06-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-bromobenzaldehyde + glycine
D-2-bromophenylserine
-
analytical yield: 6%, de: 35%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
2-chlorobenzaldehyde + glycine
D-2-chlorophenylserine
-
analytical yield: 27%, de: 67%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
2-fluorobenzaldehyde + glycine
D-2-fluorophenylserine
-
analytical yield: 68%, de: 95%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
2-nitrobenzaldehyde + glycine
D-2-nitrophenylserine
-
analytical yield: 18%, de: 65%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3,4-methylenedioxybenzaldehyde + glycine
D-3,4-methylenedioxyphenylserine
-
analytical yield: 16%, de: 46%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3-bromobenzaldehyde + glycine
D-3-bromophenylserine
-
analytical yield: 43%, de: 71%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3-chlorobenzaldehyde + glycine
D-3-chlorophenylserine
-
analytical yield: 60%, de: 85%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3-fluorobenzaldehyde + glycine
D-3-fluorophenylserine
-
analytical yield: 54%, de: 81%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3-hydroxybenzaldehyde + glycine
D-3-hydroxyphenylserine
-
analytical yield: 76%, de: 86%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
3-nitrobenzaldehyde + glycine
D-3-nitrophenylserine
-
analytical yield: 90%, de: 80%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-(methylsulfonyl)benzaldehyde + glycine
D-3-(4-methylsulfonylphenyl)serine
-
analytical yield: 63%, de: 99%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-bromobenzaldehyde + glycine
D-4-bromophenylserine
-
analytical yield: 12%, de: 74%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-chlorobenzaldehyde + glycine
D-4-chlorophenylserine
-
analytical yield: 26%, de: 86%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-fluorobenzaldehyde + glycine
D-4-fluorophenylserine
-
analytical yield: 42%, de: 91%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-formylbenzenesulfonamide + glycine
D-2-amino-3-hydroxy-3-(4-sulfamoylphenyl)-propanoic acid
-
analytical yield: 53%, de: above 90%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-hydroxybenzaldehyde + glycine
D-4-hydroxyphenylserine
-
analytical yield: 15%, de: 70%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
4-nitrobenzaldehyde + glycine
D-4-nitrophenylserine
-
analytical yield: 31%, de: 75%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
benzaldehyde + glycine
D-phenylserine
-
analytical yield: 79%, de: 98%, conditions: 1 ml solution containing glycine (1 M), benzaldehyde (or its derivate) (100 mM), pyridoxal 5'-phosphate (50 mM), MnCl2 (50 mM), and D-threonine aldolase (23 U) at 5°C, 4 h, ee >99% (D) for all reactions
-
-
?
D-alanine + 3-nitrobenzaldehyde
(betaS)-beta-hydroxy-alpha-methyl-3-nitro-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of D-alanine over 3-nitrobenzaldehyde, 3 hours test time give less than 5% yield and 80% D-isomer, 24 hours test time give less than 12% yield and 65% D-isomer
-
-
r
D-alanine + 3-nitrobenzaldehyde
beta-(3-nitrophenyl)-alpha-methyl-serine
-
-
-
-
?
D-alanine + benzaldehyde
2-amino-3-hydroxy-2-methyl-3-phenylpropanoic acid
-
-
-
-
?
D-serine + 3-nitrobenzaldehyde
beta-(3-nitrophenyl)-alpha-hydroxymethyl-serine
-
-
-
-
?
D-serine + benzaldehyde
2-amino-3-hydroxy-2-hydroxymethyl-3-phenylpropanoic acid
-
-
-
-
?
glycine + (4R)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2R,3R)-2-amino-3-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]-3-hydroxypropanoic acid + (2R,3S)-2-amino-3-[(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]-3-hydroxypropanoic acid
-
-
-
-
r
glycine + (4S)-2,2-dimethyl-1,3-dioxolane-4-carbaldehyde
(2R,3R)-2-amino-3-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]-3-hydroxypropanoic acid + (2R,3S)-2-amino-3-[(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]-3-hydroxypropanoic acid
-
-
-
-
?
glycine + 2-aminobenzaldehyde
(betaS)-2-amino-beta-hydroxy-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over benzaldehyde, 3 hours test time give less than 1% yield and no data about D-isomer, 24 hours test time give less than 1% yield and no data about D-isomer
-
-
r
glycine + 2-methylpropanal
(2R,3S)-2-amino-3-hydroxy-4-methylpentanoic acid + (2R,3R)-2-amino-3-hydroxy-4-methylpentanoic acid
-
-
-
-
r
glycine + 2-nitrobenzaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(2-nitrophenyl)propanoic acid + (2R,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
-
-
-
r
glycine + 2-nitrobenzaldehyde
(betaS)-beta-hydroxy-2-nitro-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over 2-nitrobenzaldehyde, 3 hours test time give 1% yield and no data about D-isomer, 24 hours test time give 1% yield and more than 97% D-isomer
-
-
r
glycine + 2-nitrobenzaldehyde
D-3-(2-nitrophenyl)serine
the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br
-
-
r
glycine + 3-hydroxybenzaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(3-hydroxyphenyl)propanoic acid + (2R,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
-
-
-
r
glycine + 3-hydroxybenzaldehyde
(betaS)-beta,3-dihydroxy-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over 3-hydroxybenzaldehyde, 3 hours test time give less than 1% yield, 24 hours test time give 3% yield and 70% D-isomer
-
-
r
glycine + 3-nitrobenzaldehyde
(betaS)-beta-hydroxy-3-nitro-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over 3-nitrobenzaldehyde, 3 hours test time give 20% yield and 93% D-isomer, 24 hours test time give 55% yield and 85% D-isomer
-
-
r
glycine + 4-(methylsulfonyl)benzaldehyde
D-3-(4-methylsulfonylphenyl)serine
-
-
-
r
glycine + 4-fluoro-3-nitrobenzaldehyde
(2R,3S)-2-amino-3-(4-fluoro-3-nitrophenyl)-3-hydroxypropanoic acid + (2R,3R)-2-amino-3-(4-fluoro-3-nitrophenyl)-3-hydroxypropanoic acid
-
-
-
-
r
glycine + 4-methylbenzaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(4-methylphenyl)propanoic acid + (2R,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
-
-
-
r
glycine + 4-nitrobenzaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid + (2R,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid
-
-
-
-
r
glycine + 4-nitrobenzaldehyde
(betaS)-beta-hydroxy-4-nitro-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over 4-nitrobenzaldehyde, 3 hours test time give 12% yield and 40% D-isomer, 24 hours test time give 36% yield and 40% D-isomer
-
-
r
glycine + benzaldehyde
(2R,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + (2R,3R)-2-amino-3-hydroxy-3-phenylpropanoic acid
-
-
-
-
r
glycine + benzaldehyde
(betaS)-beta-hydroxy-D-phenylalanine
-
high concentrations of both substrates and 10fold excess of glycine over benzaldehyde, 3 hours test time give 10% yield and 97% D-isomer, 24 hours test time give 17% yield and 76% D-isomer
-
-
r
glycine + benzaldehyde
D-phenylserine
the erythro isomer is obtained as the major product when the temperature is above 15°C, and lowering the temperature result in an increase in threo isomer.Water-miscible organic solvents exert limited effect on the conversion, but greatly enhance the diastereomeric excess of the product, with 10% CH3CN giving the highest diastereomeric excess. For other organic solvents (THF, ethyl acetate, 2-methoxy-2-methylpropan, 1,4-dioxane, dichloromethane and toluene), lower stereoselectivity at the beta-carbon is observed
-
-
r
glycine + butyraldehyde
(2R,3S)-2-amino-3-hydroxyhexanoic acid + (2R,3R)-2-amino-3-hydroxyhexanoic acid
-
-
-
-
r
glycine + hexanaldehyde
(2R,3R)-2-amino-3-hydroxyoctanoic acid + (2R,3S)-2-amino-3-hydroxyoctanoic acid
-
-
-
-
r
glycine + octanaldehyde
(2R,3R)-2-amino-3-hydroxydecanoic acid + (2R,3S)-2-amino-3-hydroxydecanoic acid
-
-
-
-
r
glycine + phenylacetaldehyde
(2R,3S)-2-amino-3-hydroxy-4-phenylbutanoic acid + (2R,3R)-2-amino-3-hydroxy-4-phenylbutanoic acid
-
-
-
-
r
glycine + piperonal
(3S)-3-(1,3-benzodioxol-5-yl)-D-serine
-
high concentrations of both substrates and 10fold excess of glycine over piperonal, 3 hours test time give less than 1% yield and no data about D-isomer, 24 hours test time give 5% yield and 70% D-isomer
-
-
r
glycine + pyridine-4-carboxaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
D-beta-hydroxy-alpha-aminovaleric acid
glycine + propionaldehyde
-
-
-
-
?
D-threonine
glycine + acetaldehyde
-
stereospecific for D-beta-hydroxyamino acids
-
?
glycine + 2-chlorobenzaldehyde
D-3-(2-chlorophenyl)serine
the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br
-
-
r
glycine + 2-chlorobenzaldehyde
D-3-(2-chlorophenyl)serine
the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br
-
-
r
glycine + 2-fluorobenzaldehyde
D-3-(2-fluorophenyl)serine
the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br
-
-
r
glycine + 2-fluorobenzaldehyde
D-3-(2-fluorophenyl)serine
the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br
-
-
r
glycine + acetaldehyde
D-allothreonine
-
the enzyme catalyzes the synthesis of D- and D-allothreonine from a mixture of glycine and acetaldehyde. The diastereomer excess of D-threonine is 18%
-
-
r
glycine + acetaldehyde
D-threonine
-
the enzyme catalyzes the synthesis of D- and D-allothreonine from a mixture of glycine and acetaldehyde. The diastereomer excess of D-threonine is 18%
-
-
r
glycine + pyridine-4-carboxaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
-
-
?
glycine + pyridine-4-carboxaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
Achromobacter xylosoxidans IFO 12699
-
-
-
?
glycine + pyridine-4-carboxaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
-
-
-
?
glycine + pyridine-4-carboxaldehyde
(2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
-
-
-
?
additional information
?
-
-
a high excess of glycine shifts the equilibrium toward the phenylserine side and thus 10 equiv of glycine is utilized (1 M glycine, 100 mM benzaldehyde) throughout the entire study
-
-
-
additional information
?
-
-
in a systematic study, 21 ring-substituted benzaldehydes are reacted with glycine under catalysis with a L-threonine aldolase (LTA) from Pseudomonas putida and a D-threonine aldolase (DTA) from Alcaligenes xylosoxidans to form the corresponding beta-hydroxy-alpha-amino acids
-
-
-
additional information
?
-
the enzyme shows high activity toward aromatic aldehydes with electron-withdrawing substituents. The substrate profiling indicates that the enzyme accepts a wider range of acceptor substrates and is more active toward aromatic aldehydes bearing electron-withdrawing groups than those with electron-donating substituents. Molecular docking studies suggest that the substituent on the benzene ring of the substrate is critical in determining the enzyme activity and stereoselectivity by affecting the interaction between the beta-OH-group of the substrate and the manganese ion
-
-
-
additional information
?
-
the enzyme shows high activity toward aromatic aldehydes with electron-withdrawing substituents. The substrate profiling indicates that the enzyme accepts a wider range of acceptor substrates and is more active toward aromatic aldehydes bearing electron-withdrawing groups than those with electron-donating substituents. Molecular docking studies suggest that the substituent on the benzene ring of the substrate is critical in determining the enzyme activity and stereoselectivity by affecting the interaction between the beta-OH-group of the substrate and the manganese ion
-
-
-
additional information
?
-
-
no aldol condensation of glycine with n-pentanal or 2-methylpropanal
-
-
-
additional information
?
-
-
no activity with but-2-enal, 4-hydroxybenzaldehyde
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
binds 1 mol of pyridoxal 5'-phosphate per mol of subunit, Lys59 is the cofactor binding site
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate dependent enzyme. The metal binding siteis close to the pyridoxal 5'-phosphate cofactor in the active site of the enzyme. Metal ion assisted pyridoxal 5'-phosphate-dependent mechanism
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
MnCl2
additional information
-
Mg2+ ions show no effect on both selectivity and activity
Mn2+
the role of the essential metal (manganese) ion is most likely to activate the beta-hydroxy group of the substrate for deprotonation by His193
Mn2+
-
requirement for a divalent cation, binds 1 mol Mn2+ per mol of subunit
MnCl2
metal ion-free enzyme solution shows no activity. Metal ions are required for the reaction. The highest activity is recovered with Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme completely loses activity in absence of either pyridoxal 5'-phosphate or divalent cations
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
DL-threo-beta-(3,4-methylenedioxyphenylserine)
-
pH 8.0, 30°C, with Mn2+; pH 8.0, 30°C, without Mn2+
2
DL-erythro-beta-(3,4-methylenedioxyphenylserine)
-
pH 8.0, 30°C, without Mn2+
2.5
DL-erythro-beta-(3,4-methylenedioxyphenylserine)
-
pH 8.0, 30°C, with Mn2+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
pH 5.0: about 55% of maximal activity, pH 10.0: about 45% of maximal activity, aldol addition
6 - 9.5
pH 6.0: about 65% of maximal activity, pH 9.5: about 75% of maximal activity, retro-aldol addition
6.5 - 9.5
-
D-threonine aldolase shows little activity at pH 6.0. However, by increasing the pH to 9.5 the analytical yield of D-phenylserine is doubled retaining high diastereoselectivity as compared to pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
temperature-optimum for yield, but less diastereoselectivity, origin thermophilic organism
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
only this range tested, at constant pH half of maximum yield achieved at 30°C, but 97% diastereoselectivity, at constant pH maximum yield achieved at 50°C, but only 87% diastereoselectivity
additional information
-
for the synthesis of D-phenylserine employing D-threonine aldolase, the rate of the aldol reaction is studied from 5 to 40°C. Lowering the temperature to 5°C results in an increase of diastereoselectivity (up to 98%) as well as in a higher analytical yield (79%) after 4 h
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme plays a major role in degradation of D-threonine
Show AA Sequence and Transmembrane Helices (569 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
42000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
determination of the crystal structure at 1.5 A resolution
hanging-drop vapour-diffusion method at 22°C. Analysis of the diffraction pattern shows that the crystal belongs to space group P1, with unit-cell parameters a = 64.79, b = 74.10, c = 89.94 A , alpha = 77.07, beta = 69.34, gamma = 71.93. The asymmetric unit contains four molecules of CrDTA
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alrY265A
-
alanine racemase with engineered function of D-threonine aldolase, capable of synthesizing beta-hydroxy-alpha-amino acids, stereoselectivity is comparable to that of D-threonine aldolase
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
after being incubated at various pH values for 12 h, the enzyme retains the highest activity at pH 6.0 for both retro-aldol and aldol addition reactions
747468
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
the enzyme retains about 70% activity from 25°C to 60°C after it is heated for 30 min
50
additional information
existence of the metal ions (Mn2+) enhances the thermal stability of the enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
existence of the metal ions (Mn2+) enhances the stability of the enzyme
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
-
divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, enzyme solution prepared by lysing the cells loses about 55% of its initial activity after 1 week of storage
4°C, enzyme solution prepared by lysing the cells loses about 55% of its initial activity after 1 week of storage
-
4°C, enzyme solution prepared by lysing the cells loses about 55% of its initial activity after 1 week of storage
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
synthesis
medicine
-
low-specificity threonine aldolase can be used in production of L-threo-3-[4-(methylthio)phenylserine], an intermediate for synthesis of antibiotics florfenicol and thiamphenicol
medicine
-
efficient biocatalyst for resolution of L-X-3,4-methylenedioxyphenylserine, an intermediate for production of a therapeutic drug for Parkinson's disease
medicine
-
low-specificity threonine aldolase can be used in production of L-threo-3-[4-(methylthio)phenylserine], an intermediate for synthesis of antibiotics florfenicol and thiamphenicol
-
pharmacology
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
pharmacology
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
pharmacology
the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals
pharmacology
Achromobacter xylosoxidans IFO 12699
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
-
pharmacology
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
-
synthesis
-
alanine racemase with engineered function of D-threonine aldolase, capable of synthesizing beta-hydroxy-alpha-amino acids, stereoselectivity is comparable to that of D-threonine aldolase
synthesis
the enzyme might be a promising biocatalyst for producing chiral aromatic beta-hydroxy-alpha-amino acids
synthesis
-
the enzyme can be used for the asymmetric synthesis alpha-quaternary alpha-amino acids
synthesis
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
synthesis
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
synthesis
-
the enzyme is a powerful tool for the stereospecific synthesis of various beta-hydroxy amino acids in synthetic organic chemistry
synthesis
the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals
synthesis
Achromobacter xylosoxidans IFO 12699
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
-
synthesis
-
efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization
-
synthesis
-
the enzyme might be a promising biocatalyst for producing chiral aromatic beta-hydroxy-alpha-amino acids
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, J.Q.; Odani, M.; Dairi, T.; Itoh, N.; Shimizu, S.; Yamada, H.
A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution
Appl. Microbiol. Biotechnol.
51
586-591
1999
Arthrobacter sp., Arthrobacter sp. DK-38
brenda
Liu, J.Q.; Odani, M.; Yasuoka, T.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug
Appl. Microbiol. Biotechnol.
54
44-51
2000
Achromobacter xylosoxidans
brenda
Paiardini, A.; Contestabile, R.; D'Aguanno, S.; Pascarella, S.; Bossa, F.
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes
Biochim. Biophys. Acta
1647
214-219
2003
Arthrobacter sp.
brenda
Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
Diversity of microbial threonine aldolases and their application
J. Mol. Catal. B
10
107-115
2000
Arthrobacter sp., Arthrobacter sp. DK-38
-
brenda
Kataoka, M.; Ikemi, M.; Morikawa, T.; Miyoshi, T.; Nishi, K.I.; Wada, M.; Yamada, H.; Shimizu, S.
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38
Eur. J. Biochem.
248
385-393
1997
Arthrobacter sp., Arthrobacter sp. DK-38
brenda
Kimura, T.; Vassilev, V.P.; Shen, G.J.; Wong, C.H.
Enzymic synthesis of beta-hydroxy-alpha-amino acids based on recombinant D- and L-threonine aldolases
J. Am. Chem. Soc.
119
11734-11742
1997
Xanthomonas oryzae
-
brenda
Liu, J.Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; Yamada, H.
A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38. Molecular cloning and cofactor characterization
J. Biol. Chem.
273
16678-16685
1998
Arthrobacter sp., Arthrobacter sp. (O82872), Arthrobacter sp. DK-38 (O82872)
brenda
Steinreiber, J.; Fesko, K.; Reisinger, C.; Schuermann, M.; van Assema, F.; Wolberg, M.; Mink, D.; Griengl, H.
Threonine aldolases-an emerging tool for organic synthesis
Tetrahedron
63
918-926
2006
Achromobacter xylosoxidans
-
brenda
Fesko, K.; Giger, L.; Hilvert, D.
Synthesis of beta-hydroxy-alpha-amino acids with a reengineered alanine racemase
Bioorg. Med. Chem. Lett.
18
5987-5990
2008
Geobacillus stearothermophilus
brenda
Hirato, Y.; Goto, M.; Tokuhisa, M.; Tanigawa, M.; Nishimura, K.
Crystallization and X-ray analysis of D-threonine aldolase from Chlamydomonas reinhardtii
Acta Crystallogr. Sect. F
73
86-89
2017
Chlamydomonas reinhardtii (A0A1C9ZZ39), Chlamydomonas reinhardtii
brenda
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
Pseudomonas sp.
brenda
Chen, Q.; Chen, X.; Cui, Y.; Ren, J.; Lu, W.; Feng, J.; Wu, Q.; Zhu, D.
A new D-threonine aldolase as a promising biocatalyst for highly stereoselective preparation of chiral aromatic beta-hydroxy-alpha-amino acids
Catal. Sci. Technol.
7
5964-5973
2017
Delftia sp. (A0A031HCH9), Delftia sp. RIT313 (A0A031HCH9)
-
brenda
Blesl, J.; Trobe, M.; Anderl, F.; Breinbauer, R.; Strohmeier, G.; Fesko, K.
Application of threonine aldolases for the asymmetric synthesis alpha-quaternary alpha-amino acids
ChemCatChem
53
1-7
2018
Pseudomonas sp.
-
brenda
Goldberg, S.; Goswami, A.; Guo, Z.; Chan, Y.; Lo, E.; Lee, A.; Truc, V.; Natalie, K.; Hang, C.; Rossano, L.; Schmidt, M.
Preparation of beta-hydroxy-alpha-amino acid using recombinant beta-threonine aldolase
Org. Process Res. Dev.
19
1308-1316
2015
Achromobacter xylosoxidans (Q9RBG6), Achromobacter xylosoxidans IFO 12699 (Q9RBG6), Arthrobacter sp. (O82872), Arthrobacter sp. DK-38 (O82872)
-
brenda
Hirato, Y.; Tokuhisa, M.; Tanigawa, M.; Ashida, H.; Tanaka, H.; Nishimura, K.
Cloning and characterization of D-threonine aldolase from the green alga Chlamydomonas reinhardtii
Phytochemistry
135
18-23
2017
Chlamydomonas reinhardtii (A0A1C9ZZ39), Chlamydomonas reinhardtii
brenda
Uhl, M.K.; Oberdorfer, G.; Steinkellner, G.; Riegler-Berket, L.; Mink, D.; van Assema, F.; Schuermann, M.; Gruber, K.
The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism
PLoS ONE
10
e0124056
2015
Achromobacter xylosoxidans (A0A0J9X243), Achromobacter xylosoxidans
brenda
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