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Literature summary for 3.4.24.B17 extracted from

  • Akiyama, Y.
    Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli (2002), Proc. Natl. Acad. Sci. USA, 99, 8066-8071.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.B17

Activating Compound

Activating Compound Comment Organism Structure
additional information stimulation by the proton motive force through the transmembrane region Escherichia coli
succinate stimulates, antagonist of carbonyl cyanide-3-chlorophenylhydrazone Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2,4-dinitrophenol
-
 Escherichia coli
carbonyl cyanide-3-chlorophenylhydrazone antagonist of succinate Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Escherichia coli
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Escherichia coli peptides
-
 ?
protein + H2O
-
 Escherichia coli peptides
-
 ?
protein + H2O degradation of membrane and cytoplasmic proteins Escherichia coli peptides
-
 ?

Synonyms

Synonyms Comment Organism
FtsH
-
 Escherichia coli
M41.001 Merops-ID Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli