Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (2017), Catal. Sci. Technol., 7, 5964-5973 .
No PubMed abstract available

Application

EC Number Application Comment Organism
4.1.2.42 synthesis the enzyme might be a promising biocatalyst for producing chiral aromatic beta-hydroxy-alpha-amino acids Delftia sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.42 expressed in Escherichia coli BL21 (DE3) Delftia sp.

General Stability

EC Number General Stability Organism
4.1.2.42 existence of the metal ions (Mn2+) enhances the stability of the enzyme Delftia sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.42 0.35
-
 D-allo-threonine pH 6.0, 50°C Delftia sp.
4.1.2.42 0.83
-
 D-threonine pH 6.0, 50°C Delftia sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.42 MnCl2 metal ion-free enzyme solution shows no activity. Metal ions are required for the reaction. The highest activity is recovered with Mn2+ Delftia sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.42 47000
-
 gel filtration Delftia sp.

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.42 Delftia sp. A0A031HCH9
-
-
4.1.2.42 Delftia sp. RIT313 A0A031HCH9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.42
-
 Delftia sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.2.42 21.3
-
 pH 6.0, 50°C Delftia sp.

Storage Stability

EC Number Storage Stability Organism
4.1.2.42 -80°C, recombinant His-tagged enzyme remains stable for 6 months Delftia sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.42 D-allo-threonine
-
 Delftia sp. glycine + acetaldehyde
-
 ?
4.1.2.42 D-allo-threonine
-
 Delftia sp. RIT313 glycine + acetaldehyde
-
 ?
4.1.2.42 D-threonine
-
 Delftia sp. glycine + acetaldehyde
-
 r
4.1.2.42 D-threonine
-
 Delftia sp. RIT313 glycine + acetaldehyde
-
 r
4.1.2.42 glycine + 2-chlorobenzaldehyde the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br Delftia sp. D-3-(2-chlorophenyl)serine
-
 r
4.1.2.42 glycine + 2-chlorobenzaldehyde the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br Delftia sp. RIT313 D-3-(2-chlorophenyl)serine
-
 r
4.1.2.42 glycine + 2-fluorobenzaldehyde the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br Delftia sp. D-3-(2-fluorophenyl)serine
-
 r
4.1.2.42 glycine + 2-nitrobenzaldehyde the reaction conversion and the diastereomeric excess of the 2-substituted substrates decrease in the order of F, H, Cl, Br Delftia sp. D-3-(2-nitrophenyl)serine
-
 r
4.1.2.42 glycine + 3-chlorobenzaldehyde
-
 Delftia sp. D-3-(3-chlorophenyl)serine
-
 r
4.1.2.42 glycine + 3-fluorobenzaldehyde
-
 Delftia sp. D-3-(3-fluorophenyl)serine
-
 r
4.1.2.42 glycine + 3-nitrobenzaldehyde
-
 Delftia sp. D-3-(3-nitrophenyl)serine
-
 r
4.1.2.42 glycine + 4-(methylsulfonyl)benzaldehyde
-
 Delftia sp. D-3-(4-methylsulfonylphenyl)serine
-
 r
4.1.2.42 glycine + 4-fluorobenzaldehyde
-
 Delftia sp. D-3-(4-fluorophenyl)serine
-
 r
4.1.2.42 glycine + 4-nitrobenzaldehyde
-
 Delftia sp. D-3-(4-nitrophenyl)serine
-
 r
4.1.2.42 glycine + acetaldehyde
-
 Delftia sp. D-allothreonine
-
 r
4.1.2.42 glycine + acetaldehyde
-
 Delftia sp. D-threonine
-
 r
4.1.2.42 glycine + benzaldehyde 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 Delftia sp. (2R,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + (2R,3R)-2-amino-3-hydroxy-3-phenylpropanoic acid
-
 r
4.1.2.42 glycine + benzaldehyde 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 Delftia sp. RIT313 (2R,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid + (2R,3R)-2-amino-3-hydroxy-3-phenylpropanoic acid
-
 r
4.1.2.42 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 Delftia sp. ?
-
 ?
4.1.2.42 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 Delftia sp. RIT313 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.2.42 monomer 1 * 47000, SDS-PAGE Delftia sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.2.42 25
-
 assay at Delftia sp.
4.1.2.42 50 60 aldol addition Delftia sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.2.42 additional information
-
 existence of the metal ions (Mn2+) enhances the thermal stability of the enzyme Delftia sp.
4.1.2.42 25 60 the enzyme retains about 70% activity from 25°C to 60°C after it is heated for 30 min Delftia sp.
4.1.2.42 70
-
 30 min, 50% loss of activity Delftia sp.
4.1.2.42 80
-
 30 min, 70% loss of activity Delftia sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.2.42 0.25
-
 D-allo-threonine pH 6.0, 50°C Delftia sp.
4.1.2.42 0.39
-
 D-threonine pH 6.0, 50°C Delftia sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.2.42 6
-
 aldol addition Delftia sp.
4.1.2.42 8
-
 retro-aldol addition Delftia sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.2.42 5 10 pH 5.0: about 55% of maximal activity, pH 10.0: about 45% of maximal activity, aldol addition Delftia sp.
4.1.2.42 6 9.5 pH 6.0: about 65% of maximal activity, pH 9.5: about 75% of maximal activity, retro-aldol addition Delftia sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.2.42 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 Delftia sp.

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.42 pyridoxal 5'-phosphate dependent on Delftia sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.2.42 0.47
-
 D-threonine pH 6.0, 50°C Delftia sp.
4.1.2.42 0.71
-
 D-allo-threonine pH 6.0, 50°C Delftia sp.