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Literature summary for 3.4.24.B17 extracted from

  • Okuno, T.; Yamada-Inagawa, T.; Karata, K.; Yamanaka, K.; Ogura, T.
    Spectrometric analysis of degradation of a physiological substrate sigma32 by Escherichia coli AAA protease FtsH (2004), J. Struct. Biol., 146, 148-154.
    View publication on PubMed
Search for more literature for 3.4.24.B17

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Protein + H2O Escherichia coli the enzyme can unfold proteins with lower Tms such as glutathione S-transferase (Tm: 52°C) ?
-
 ?
sigma32 + H2O Escherichia coli hydrolyzes about 140 ATP molecules during the degradation of a single molecule of cy2-sigma32. Degradation of sigma32 proceeds from the N-terminus to the C-terminus ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Protein + H2O the enzyme can unfold proteins with lower Tms such as glutathione S-transferase (Tm: 52°C) Escherichia coli ?
-
 ?
sigma32 + H2O
-
 Escherichia coli ?
-
 ?
sigma32 + H2O hydrolyzes about 140 ATP molecules during the degradation of a single molecule of cy2-sigma32. Degradation of sigma32 proceeds from the N-terminus to the C-terminus Escherichia coli ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0083
-
 sigma32
-
 Escherichia coli