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Literature summary extracted from

  • Asahara, Y.; Atsuta, K.; Motohashi, K.; Taguchi, H.; Yohda, M.; Yoshida, M.
    FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues (2000), J. Biochem., 127, 931-937.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.B17 alpha-casein temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess Thermus thermophilus
3.4.24.B17 Pepsin temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess Thermus thermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B17 T.ftsH gene, DNA determination and analysis, expression as His-tagged protein in Escherichia coli Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B17 ADP strong, complete inhibition at equimolar amounts to ATP Thermus thermophilus
3.4.24.B17 additional information no inhibition by AMP Thermus thermophilus
3.4.24.B17 o-phenanthroline chelator for divalent metal ions Thermus thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 membrane integral Thermus thermophilus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ dependent on Thermus thermophilus

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 Thermus thermophilus
-
 peptides
-
 ?
3.4.24.B17 protein + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Thermus thermophilus Q5SI82
-
-
3.4.24.B17 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SI82
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B17 recombinant His-tagged enzyme from Escherichia coli Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B17 proteolytic degradation of proteins soluble C-terminal domain harbors the ATPase and protease activity, the N-terminal domain permits the indispensible membrane integration of the enzyme, cleavage of small peptides from the C-terminal side of hydrophobic residues, overview Thermus thermophilus
a

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 additional information
-
-
 Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 largely unfolded alpha-lactalbumin + H2O no activity with the native protein, cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates Thermus thermophilus peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 additional information no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA Thermus thermophilus ?
-
 ?
3.4.24.B17 additional information no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
 ?
3.4.24.B17 protein + H2O
-
 Thermus thermophilus peptides
-
 ?
3.4.24.B17 protein + H2O cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview Thermus thermophilus peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 protein + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides
-
 ?
3.4.24.B17 protein + H2O cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 unfolded alpha-casein + H2O
-
 Thermus thermophilus peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 unfolded alpha-casein + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 unfolded pepsin + H2O cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates Thermus thermophilus peptides between 10 and 30 kDa, no large intermediates ?
3.4.24.B17 unfolded pepsin + H2O cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides between 10 and 30 kDa, no large intermediates ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 M41.001 Merops-ID Thermus thermophilus
3.4.24.B17 T.ftsH
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B17 65
-
 ATPase activity, recombinant enzyme Thermus thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.24.B17 36 70 5% of maximal activity at 36°C, 17% of maximal activity at 50°C, 63% of maximal activity at 60°C, and 67% of maximal activity at 70°C Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.B17 0.65
-
 ATP recombinant enzyme Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 ATP dependent on Thermus thermophilus
3.4.24.B17 CTP can substitute for ATP by 74% Thermus thermophilus
3.4.24.B17 GTP can substitute for ATP by 19% Thermus thermophilus
3.4.24.B17 additional information no activity with TTP, UTP, AMP, and ADP Thermus thermophilus