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Literature summary for 1.16.1.9 extracted from

  • Miethke, M.; Hou, J.; Marahiel, M.
    The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli (2011), Biochemistry, 50, 10951-10964.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
K55A the mutant shows strongly reduced activity compared to the wild type enzyme Escherichia coli
R130A the mutant shows strongly reduced activity compared to the wild type enzyme Escherichia coli
R246A the variant is rather unstable, showing precipitate formation and cofactor release during protein concentration Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
Fe(III)-enterobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0014
-
Fe(III)-vibriobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0018
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0042
-
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0059
-
Fe(III)-enterobactin mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0078
-
Fe(III)-enterobactin mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.0134
-
Fe(III)-dicitrate wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.036
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.04
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.048
-
Fe(III)-aerobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.051
-
Fe(III)-dicitrate mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.066
-
Fe(III)-dicitrate mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Strep-Tactin column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 + NADPH + H+
-
Escherichia coli Fe(II) + (2,3-dihydroxybenzoyl-Gly-Thr)3 + NADP+
-
?
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 + NADPH + H+
-
Escherichia coli Fe(II) + (2,3-dihydroxybenzoyl-L-serine)3 + NADP+
-
?
Fe(III)-aerobactin + NADPH + H+
-
Escherichia coli Fe(II) + aerobactin + NADP+
-
?
Fe(III)-bacillibactin + NADPH + H+
-
Escherichia coli Fe(II) + bacillibacitin + NADP+
-
?
Fe(III)-dicitrate + NADPH + H+
-
Escherichia coli Fe(II) + citrate + NADP+
-
?
Fe(III)-enterobactin + NADPH + H+
-
Escherichia coli Fe(II) + enterobactin + NADP+
-
?
Fe(III)-vibriobactin + NADPH + H+
-
Escherichia coli Fe(II) + vibriobactin + NADP+
-
?

Synonyms

Synonyms Comment Organism
ferric siderophore reductase
-
Escherichia coli
YqjH
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD
-
Escherichia coli
NADPH
-
Escherichia coli

General Information

General Information Comment Organism
malfunction the absence of YqjH slows growth Escherichia coli
metabolism YqjH represents a redox factor that enhances the efficiency of ferric iron assimilation during siderophore-dependent iron homeostasis and enhances siderophore utilization in different iron acquisition pathways, including assimilation of low-potential ferric substrates that are not reduced by common cellular cofactors Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.02
-
Fe(III)-aerobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.032
-
Fe(III)-enterobactin mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.076
-
Fe(III)-enterobactin mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.091
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.132
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.139
-
Fe(III)-dicitrate mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
0.271
-
Fe(III)-dicitrate mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
1.268
-
Fe(III)-vibriobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
5.427
-
Fe(III)-dicitrate wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
8.211
-
Fe(III)-enterobactin wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
9.193
-
Fe(III)-(N-2,3-dihydroxybenzoyl-Gly-Thr)3 wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli
23.35
-
Fe(III)-(N-2,3-dihydroxybenzoyl-L-serine)3 wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C Escherichia coli