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Literature summary extracted from

  • Wieteska, L.; Ionov, M.; Szemraj, J.; Feller, C.; Kolinski, A.; Gront, D.
    Improving thermal stability of thermophilic L-threonine aldolase from Thermotoga maritima (2015), J. Biotechnol., 199, 69-76 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.2.5 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 Thermotoga maritima

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.5 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) Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.5 A21C L-threonine cleavage activity is similar to the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 F85Y L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 I124D L-threonine cleavage activity is about 65% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 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 Thermotoga maritima
4.1.2.5 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 Thermotoga maritima
4.1.2.5 Q22K L-threonine cleavage activity is about 75% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 S198D L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 T59D L-threonine cleavage activity is about 10% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 V235C L-threonine cleavage activity is about 110% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 V29D L-threonine cleavage activity is about 90% of the activity of the wild-type enzyme Thermotoga maritima
4.1.2.5 W86E the mutant enzyme displays enhanced activity, with stability similar to the wild type enzyme Thermotoga maritima

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.5 37000
-
 SDS-PAGE Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.5 Thermotoga maritima Q9X266
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.5 glycine + acetaldehyde
-
 Thermotoga maritima L-threonine
-
 r
4.1.2.5 L-threonine
-
 Thermotoga maritima glycine + acetaldehyde
-
 r

Subunits

EC Number Subunits Comment Organism
4.1.2.5 tetramer 4 * 37000, SDS-PAGE Thermotoga maritima

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.2.5 75
-
-
 Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.2.5 75
-
 15 h, 50% loss of activity Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.5 pyridoxal 5'-phosphate dependent on Thermotoga maritima