Literature summary for 4.1.2.5 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 .

Search for more literature for 4.1.2.5

Application

Application	Comment	Organism
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)

Cloned (Comment)	Organism
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

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

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9X266	-	-

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Cofactor

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

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Release 2023.1 (January 2023)