Literature summary for 1.17.1.9 extracted from

Hartmann, T.; Schrapers, P.; Utesch, T.; Nimtz, M.; Rippers, Y.; Dau, H.; Mroginski, M.A.; Haumann, M.; Leimkuehler, S.
The molybdenum active site of formate dehydrogenase is capable of catalyzing C-H bond cleavage and oxygen atom transfer reactions (2016), Biochemistry, 55, 2381-2389.

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Protein Variants

Protein Variants	Comment	Organism
C386S	inactive	Rhodobacter capsulatus
H387F	inactive	Rhodobacter capsulatus
H387K	the mutant shows about 6200fold decreased catalytic efficiency compared to the wild type enzyme	Rhodobacter capsulatus
H387M	the mutant shows about 20fold decreased catalytic efficiency compared to the wild type enzyme	Rhodobacter capsulatus
H387M/R587T	inactive	Rhodobacter capsulatus
H387R	inactive	Rhodobacter capsulatus
R587K	the mutant shows about 6200fold decreased catalytic efficiency compared to the wild type enzyme	Rhodobacter capsulatus
R587T	inactive	Rhodobacter capsulatus

Inhibitors

Inhibitors	Comment	Organism	Structure
iodoacetamide	-	Rhodobacter capsulatus
nitrate	competitive inhibitor	Rhodobacter capsulatus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.19	-	formate	wild type enzyme, at pH 9.0 and 25°C	Rhodobacter capsulatus
3.6	-	formate	mutant enzyme H387M, at pH 9.0 and 25°C	Rhodobacter capsulatus
27.5	-	formate	mutant enzyme H387K, at pH 9.0 and 25°C	Rhodobacter capsulatus
362	-	formate	mutant enzyme R587K, at pH 9.0 and 25°C	Rhodobacter capsulatus

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
formate + NAD+	-	Rhodobacter capsulatus	CO2 + NADH + H+	-	?
additional information	the enzyme also exhibits nitrate reductase activity with methyl viologen as cosubstrate	Rhodobacter capsulatus	?	-	?

Synonyms

Synonyms	Comment	Organism
FDH	-	Rhodobacter capsulatus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.9	-	formate	mutant enzyme H387K, at pH 9.0 and 25°C	Rhodobacter capsulatus
11.2	-	formate	mutant enzyme R587K, at pH 9.0 and 25°C	Rhodobacter capsulatus
33.7	-	formate	mutant enzyme H387M, at pH 9.0 and 25°C	Rhodobacter capsulatus
35.4	-	formate	wild type enzyme, at pH 9.0 and 25°C	Rhodobacter capsulatus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	-	-	Rhodobacter capsulatus

Cofactor

Cofactor	Comment	Organism	Structure
molybdenum cofactor	-	Rhodobacter capsulatus
NAD+	-	Rhodobacter capsulatus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
1.6	-	nitrate	wild type enzyme, at pH 9.0 and 25°C	Rhodobacter capsulatus

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.032	-	formate	mutant enzyme R587K, at pH 9.0 and 25°C	Rhodobacter capsulatus
0.033	-	formate	mutant enzyme H387K, at pH 9.0 and 25°C	Rhodobacter capsulatus
9.38	-	formate	mutant enzyme H387M, at pH 9.0 and 25°C	Rhodobacter capsulatus
186.4	-	formate	wild type enzyme, at pH 9.0 and 25°C	Rhodobacter capsulatus

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Release 2023.1 (January 2023)