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Literature summary for 3.4.24.B17 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
Search for more literature for 3.4.24.B17

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

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

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral Thermus thermophilus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent on Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Thermus thermophilus
-
 peptides
-
 ?
protein + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SI82
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SI82
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli Thermus thermophilus

Reaction

Reaction Comment Organism Reaction ID
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
additional information no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA Thermus thermophilus ?
-
 ?
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 ?
-
 ?
protein + H2O
-
 Thermus thermophilus peptides
-
 ?
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 ?
protein + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides
-
 ?
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 ?
unfolded alpha-casein + H2O
-
 Thermus thermophilus peptides between 10 and 30 kDa, no large intermediates ?
unfolded alpha-casein + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 peptides between 10 and 30 kDa, no large intermediates ?
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 ?
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

Synonyms Comment Organism
M41.001 Merops-ID Thermus thermophilus
T.ftsH
-
 Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 ATPase activity, recombinant enzyme Thermus thermophilus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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]

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

Cofactor

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