Literature summary for 2.7.9.3 extracted from

Kim, I.Y.; Veres, Z.; Stadtman, T.C.
Biochemical analysis of Escherichia coli selenophosphate synthetase mutants (1993), J. Biol. Chem., 268, 27020-27025.

Search for more literature for 2.7.9.3

Protein Variants

Protein Variants	Comment	Organism
C17S	no catalytic activity	Escherichia coli
C17S/C19S	no catalytic activity	Escherichia coli
C19S	-	Escherichia coli
G18V	70% reduced activity, 4fold-increase in the Km-value for ATP compared to that of the wild type enzyme	Escherichia coli
H13N	unaltered activity level, no substantially altered Km-value for ATP compared to that of the wild type enzyme	Escherichia coli
K20Q	no catalytic activity	Escherichia coli
K20R	nearly no remaining activity	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
8-azido-ATP	-	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.9	-	ATP	wild type enzyme	Escherichia coli
0.9	-	ATP	pH 7.2, 37°C	Escherichia coli
1.2	-	ATP	pH 7.2, 37°C	Escherichia coli
1.2	-	ATP	mutant H13N	Escherichia coli
4	-	ATP	pH 7.2, 37°C	Escherichia coli
4	-	ATP	mutant G18V	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	altered binding by cysteine mutants	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild type and mutant enzymes	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + selenide + H2O	-	Escherichia coli	AMP + selenophosphate + phosphate	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.95	-	8-azido-ATP	pH 7.2, 37°C	Escherichia coli

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Release 2023.1 (January 2023)