Literature summary for 1.17.1.9 extracted from

Tishkov, V.I.; Matorin, A.D.; Rojkova, A.M.; Fedorchuk, V.V.; Savitsky, P.A.; Dementieva, L.A.; Lamzin, V.S.; Mezentzev, A.V.; Popov, V.O.
Site-directed mutagenesis of the formate dehydrogenase active center: role of the His332-Gln313 pair in enzyme catalysis (1996), FEBS Lett., 390, 104-108.

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Protein Variants

Protein Variants	Comment	Organism
H332F	complete loss of activity. The mutant is still able to bind coenzyme, but not substrate or analogues	Pseudomonas sp.
Q313E	mutation shifts the pK of the group controlling formate binding from less than 5.5 in wild-type enzyme to 7.6	Pseudomonas sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
N3-	-	Pseudomonas sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.07	-	NAD+	wild-type enzyme and mutant enzyme Q313E	Pseudomonas sp.
4	-	formate	mutant enzyme Q313E	Pseudomonas sp.
7	-	formate	wild-type enzyme	Pseudomonas sp.

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
formate + NAD+	-	Pseudomonas sp.	CO2 + NADH + H+	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Pseudomonas sp.

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Release 2023.1 (January 2023)