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Literature summary extracted from

  • Bruckner, R.C.; Gunyuzlu, P.L.; Stein, R.L.
    Coupled kinetics of ATP and peptide hydrolysis by Escherichia coli FtsH protease (2003), Biochemistry, 42, 10843-10852.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B17 ftsH gene, expression as His-tagged enzyme in strain BL21(DE3) Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B17 EDTA
-
 Escherichia coli
3.4.24.B17 additional information no inhibition by phenylmethylsulfonylfluoride Escherichia coli
3.4.24.B17 o-phenanthroline
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.B17 additional information
-
 additional information kinetics Escherichia coli
3.4.24.B17 0.021
-
 ATP with FGH-NO2FFAF-methoxy, pH 8.0, 37°C Escherichia coli
3.4.24.B17 0.023
-
 protein sigma32 pH 8.0, 42°C Escherichia coli
3.4.24.B17 0.023
-
 ATP with protein sigma32, pH 8.0, 37°C Escherichia coli
3.4.24.B17 0.104
-
 CTP pH 8.0, 37°C Escherichia coli
3.4.24.B17 7.3
-
 GTP pH 8.0, 37°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 cytoplasmic membrane integral, schematic model of structure and arrangement in the membane Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ dependent on Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B17 additional information
-
 the large complexes exhibit either ATPase and protease activity, while smaller ones do not Escherichia coli
3.4.24.B17 70000
-
 x * 70000, SDS-PAGE 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 involved in the degradation of regulatory proteins and uncomplexed subunits of membrane protein complexes 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 enzyme, solubilization by N-lauylsarcosine, refolding in presence of ATP, Mg2+ and Zn2+, and purification to near homogeneity Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B17 proteolytic degradation of proteins mechanism Escherichia coli
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.4.24.B17 recombinant enzyme, solubilization by N-lauylsarcosine, refolding in presence of ATP, Mg2+ and Zn2+, and purification to near homogeneity, the refolded enzyme has properties similar to the overexpressed solubilized one Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.B17 0.0036
-
 purified recombinant refolded enzyme, substrate protein sigma32 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 CTP + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 FGH-(NO2)FFAF-methyl ester + H2O exclusively cleaved at the (NO2)Phe-Phe bond Escherichia coli FGH-(NO2)F + Phe-Ala-Phe-methyl ester
-
 ?
3.4.24.B17 GTP + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 additional information large complexes exhibit either ATPase and protease activity, while smaller ones do not Escherichia coli ?
-
 ?
3.4.24.B17 protein + H2O
-
 Escherichia coli peptides
-
 ?
3.4.24.B17 protein + H2O involved in the degradation of regulatory proteins and uncomplexed subunits of membrane protein complexes Escherichia coli peptides
-
 ?
3.4.24.B17 protein SecY + H2O uncomplexed subunit of the protein translocase Escherichia coli ?
-
 ?
3.4.24.B17 protein sigma32 + H2O regulatory protein Escherichia coli peptides approximately 10 peptides with MW below 3 kDa ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 multimer x * 70000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 FtsH
-
 Escherichia coli
3.4.24.B17 FtsH protease
-
 Escherichia coli
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 42
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.B17 0.003
-
 protein sigma32 pH 8.0, 42°C Escherichia coli
3.4.24.B17 0.023
-
 ATP with FGH-NO2FFAF-methoxy, pH 8.0, 37°C Escherichia coli
3.4.24.B17 0.3
-
 ATP with protein sigma32, pH 8.0, 37°C Escherichia coli
3.4.24.B17 0.32
-
 CTP pH 8.0, 37°C Escherichia coli
3.4.24.B17 0.53
-
 GTP pH 8.0, 37°C Escherichia coli
3.4.24.B17 6.08
-
 GTP pH 8.0, 37°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B17 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 2',3'-dideoxy-ATP
-
 Escherichia coli
3.4.24.B17 2',3'-dideoxy-CTP
-
 Escherichia coli
3.4.24.B17 2'-deoxy-ATP
-
 Escherichia coli
3.4.24.B17 3'-deoxy-ATP
-
 Escherichia coli
3.4.24.B17 7-daza-2'-deoxy-ATP low activity Escherichia coli
3.4.24.B17 ATP
-
 Escherichia coli
3.4.24.B17 ATPalphaS low activity Escherichia coli
3.4.24.B17 CTP
-
 Escherichia coli
3.4.24.B17 dCTP
-
 Escherichia coli
3.4.24.B17 additional information no activity with ATPgammaS, absolutely dependent on nucleoside 5'-triphosphates like ATP or CTP, not GTP or UTP, or derivatives Escherichia coli