Literature summary for 2.1.1.148 extracted from

Leduc, D.; Graziani, S.; Lipowski, G.; Marchand, C.; Le Marechal, P.; Liebl, U.; Myllykallio, H.
Functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers (2004), Proc. Natl. Acad. Sci. USA, 101, 7252-7257.

Search for more literature for 2.1.1.148

Protein Variants

Protein Variants	Comment	Organism
H48Q	inactive mutant enzyme	Helicobacter pylori
H48Q/S84A	inactive mutant enzyme	Helicobacter pylori
H48Q/S84C	inactive mutant enzyme	Helicobacter pylori
R74A	the KM-value for dUMP is 5.1fold higher than the wild-type value, the turnover-number is 4.6fold lower than the wild-type value	Helicobacter pylori
R74K	the KM-value for dUMP is nearly identical to wild-type value, the turnover-number is 6.6fold lower than the wild-type value	Helicobacter pylori
S84A	the KM-value for dUMP is 5.3fold higher than the wild-type value, the turnover-number is 2.1fold lower than the wild-type value. Mutation abolishes thymidylate synthase activity in vivo	Helicobacter pylori
S84A/S85A	inactive mutant enzyme	Helicobacter pylori
S84C	mutation abolishes thymidylate synthase activity in vivo	Helicobacter pylori
S84Y	the KM-value for dUMP is 1.9fold higher than the wild-type value, the turnover-number is 1.6fold lower than the wild-type value	Helicobacter pylori
Y87F	the KM-value for dUMP is 1.8fold lower than the wild-type value, the turnover-number is nearly identical to the wild-type value	Helicobacter pylori

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers. The active-site configurations of ThyX proteins, present in many human pathogenic bacteria, and of human thymidylate synthase A (EC 2.1.1.45) are different.	Helicobacter pylori

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.00083	-	dUMP	mutant enzyme S84C	Helicobacter pylori
0.0012	-	dUMP	mutant enzyme R74K	Helicobacter pylori
0.0017	-	dUMP	mutant enzyme R74A	Helicobacter pylori
0.0037	-	dUMP	mutant enzyme S84A	Helicobacter pylori
0.0076	-	dUMP	wild-type enzyme	Helicobacter pylori
0.008	-	dUMP	mutant enzyme Y87F	Helicobacter pylori
0.012	-	dUMP	mutant enzyme S84Y	Helicobacter pylori

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Helicobacter pylori

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5,10-methylenetetrahydrofolate + dUMP + FADH2	-	Helicobacter pylori	dTMP + tetrahydrofolate + FAD	-	?

Subunits

Subunits	Comment	Organism
?	x * 27168.2, wild-type enzyme, MALDI-TOF	Helicobacter pylori

Synonyms

Synonyms	Comment	Organism
thymidylate synthase X	-	Helicobacter pylori
ThyX	-	Helicobacter pylori

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0038	-	dUMP	mutant enzyme Y87F	Helicobacter pylori
0.0072	-	dUMP	wild-type enzyme	Helicobacter pylori
0.0078	-	dUMP	mutant enzyme R74K	Helicobacter pylori
0.0097	-	dUMP	mutant enzyme S84Y	Helicobacter pylori
0.037	-	dUMP	mutant enzyme R74A	Helicobacter pylori
0.0384	-	dUMP	mutant enzyme S84A	Helicobacter pylori
0.14	-	dUMP	mutant enzyme S84C	Helicobacter pylori

Cofactor

Cofactor	Comment	Organism	Structure
FAD	wild-type and mutant enzymes Y87F, S84Y, H48Q, S84A and S84C contain quantities of tightly bound FAD. Mutant enzymes R74A, R74K, H48Q/S84A and H48Q/S84C easily lose considerable amounts of bound FAD	Helicobacter pylori

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Release 2023.1 (January 2023)