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Literature summary for 1.11.1.26 extracted from

  • Dip, P.V.; Kamariah, N.; Subramanian Manimekalai, M.S.; Nartey, W.; Balakrishna, A.M.; Eisenhaber, F.; Eisenhaber, B.; Gruber, G.
    Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli (2014), Acta Crystallogr. Sect. D, 70, 2848-2862 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour diffusion method at 23°C. Crystal structures of both of the subunits of EcAhpR, EcAhpF and EcAhpC, are solved. The EcAhpF structures (2.0 and 2.65 A resolution) reveal an open and elongated conformation, while that of EcAhpC (3.3 A resolution) forms a decameric ring Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE08 AND P35340 P0AE08: subunit C (ahpC), P35340: subunit F (ahpF)
-
Escherichia coli K12 P0AE08 AND P35340 P0AE08: subunit C (ahpC), P35340: subunit F (ahpF)
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H2O2
-
Escherichia coli NAD+ + 2 H2O
-
?
NADH + H2O2
-
Escherichia coli K12 NAD+ + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
AhpC gene name of subunit C Escherichia coli
AhpF gene name of subunit f Escherichia coli
AhpR
-
Escherichia coli
alkylhydroperoxide reductase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Escherichia coli