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Literature summary extracted from

  • Akiyama, Y.; Ito, K.
    Roles of homooligomerization and membrane association in ATPase and proteolytic activities of FtsH in vitro (2001), Biochemistry, 40, 7687-7693.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.B17 dimethylsulfoxid induces conformational changes, stimulates with SecY s substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B17 expression of His-Myc-tagged wild-type and mutant enzymes from strain TY024 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.B17 additional information construction of mutants by deletion of N-terminal membrane region, replacement by a leucine-zipper, or replacement by a lactose permease transmembrane segment, the matated proteins show very low remaining activity, but are stimulated by dimethylsulfoxide, the deletion mutant does not show ATPase and proteolytic activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B17 ATP inhibitory at high concentration in presence of dimethylsulfoxide Escherichia coli
3.4.24.B17 Dimethylsulfoxide induces conformational changes, stimulates with SecY as substrate, at concentration up to 20% v/v, slightly inhibitory with casein as a substrate Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 cytoplasmic membrane the N-terminus mediates membrane association as well as homooligomeric interaction Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 additional information metalloprotease Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B17 protein + H2O Escherichia coli
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B17 recombinant His-Myc-tagged wild-type and mutant enzymes Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B17 proteolytic degradation of proteins degradation of soluble and integral membrane proteins Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 casein + H2O resorufin-labeled substrate Escherichia coli ?
-
 ?
3.4.24.B17 PhoA protein + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein + H2O
-
 Escherichia coli peptides
-
 ?
3.4.24.B17 protein + H2O substrate binding by the cytoplasmic domain Escherichia coli peptides
-
 ?
3.4.24.B17 SecY protein + H2O
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 More the N-terminus mediates membrane association as well as homooligomeric interaction Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 M41.001 Merops-ID Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B17 37
-
 ATPase activity assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B17 8.1
-
 ATPase activity assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 ATP dependent on, induces conformational changes by binding irrespective of ATP hydrolysis Escherichia coli