Literature summary for 2.1.1.148 extracted from

Krumova, S.; Todinova, S.; Tileva, M.; Bouzhir-Sima, L.; Vos, M.H.; Liebl, U.; Taneva, S.G.
Thermal stability and binding energetics of thymidylate synthase ThyX (2016), Int. J. Biol. Macromol., 91, 560-567 .

Search for more literature for 2.1.1.148

Protein Variants

Protein Variants	Comment	Organism
S88W	no binding of dUMP observed	Thermotoga maritima
Y91F	similar to wild-type, at saturating FAD conditions dUMP binding to the protein/FAD complex leads to additional stabilization by about 7 degrees	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Paramecium bursaria Chlorella virus 1	O41156	-	-
Thermotoga maritima	Q9WYT0	-	-
Thermotoga maritima DSM 3109	Q9WYT0	-	-

Synonyms

Synonyms	Comment	Organism
A674R	-	Paramecium bursaria Chlorella virus 1
ThyX	-	Thermotoga maritima
ThyX	-	Paramecium bursaria Chlorella virus 1

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
56.1	-	melting temperature	Paramecium bursaria Chlorella virus 1
100.4	-	melting temperature, mutant S88W	Thermotoga maritima
102.4	-	melting temperature, wild-type	Thermotoga maritima
103.1	-	melting temperature, mutant Y91F	Thermotoga maritima
107.2	-	melting temperature, mutant S88W, presence of FAD	Thermotoga maritima
107.3	-	melting temperature, wild-type, presence of FAD	Thermotoga maritima
107.4	-	melting temperature, mutant Y91F, presence of FAD	Thermotoga maritima

Cofactor

Cofactor	Comment	Organism	Structure
FAD	presence of FAD additionally stabilizes the protein against thermal denaturation by 10 degrees. The assembly of thymidylate synthase with FAD is governed by a large enthalpy change opposed by an unfavorable entropy change resulting in a relatively strong nanomolar binding	Paramecium bursaria Chlorella virus 1
FAD	presence of FAD additionally stabilizes the protein against thermal denaturation by 4.9 degrees. Binding of dUMP to FAD-loaded proteins stabilizes further. ThyX binds FAD with a low micromolar binding affinity in a process characterized by a favorable entropy change	Thermotoga maritima

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)