Literature summary for 1.7.5.1 extracted from

Bertero, M.G.; Rothery, R.A.; Boroumand, N.; Palak, M.; Blasco, F.; Ginet, N.; Weiner, J.H.; Strynadka, N.C.
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A (2005), J. Biol. Chem., 280, 14836-14843.

Search for more literature for 1.7.5.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of Escherichia coli nitrate reductase A in complex with pentachlorophenol is determined to 2.0 A of resolution	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
K86A	mutant has a lower plumbagin:nitrate oxidoreductase activity than the wild-type enzyme, 10/s compared with 68/s, respectively	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
2-n-heptyl-4-hydroxyquinoline N-oxide	-	Escherichia coli
Pentachlorophenol	mixed inhibition	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.147	-	5-hydroxy-2-methyl-naphthalene-1,4-diol	pH 7.0	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol	i.e. reduced form of plumbagin	Escherichia coli	nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O	i.e. plumbagin	?

Synonyms

Synonyms	Comment	Organism
NarGHI	-	Escherichia coli
quinol:nitrate oxidoreductase	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
10	-	nitrate	mutant enzyme K86A	Escherichia coli
68	-	nitrate	wild-type enzyme	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
additional information	molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.057	-	Pentachlorophenol	pH 7.0, competitive inhibition constant	Escherichia coli
0.49	-	Pentachlorophenol	pH 7.0, uncompetitive inhibition constant	Escherichia coli

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0004	-	pH 7.0	Escherichia coli	Pentachlorophenol
0.0015	-	pH 7.0	Escherichia coli	2-n-heptyl-4-hydroxyquinoline N-oxide

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)