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Literature summary for 3.4.21.111 extracted from

  • Marie-Claire, C.; Yabuta, Y.; Suefuji, K.; Matsuzawa, H.; Shinde, U.
    Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide (2001), J. Mol. Biol., 305, 151-165.
    View publication on PubMed
Search for more literature for 3.4.21.111

Cloned(Commentary)

Cloned (Comment) Organism
ProA peptide Thermus aquaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12090
-
 ProA peptide, calculated from nucleic acid sequence Thermus aquaticus
14000
-
 ProA peptide, gel filtration Thermus aquaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermus aquaticus requires its propeptide ProA to function as an intramolecular chaperone, N-terminal IMC can inhibit aqualysin activity and form a stable complex with subtilisin BPN' ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ProA peptide Thermus aquaticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information requires its propeptide ProA to function as an intramolecular chaperone, N-terminal IMC can inhibit aqualysin activity and form a stable complex with subtilisin BPN' Thermus aquaticus ?
-
 ?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O synthetic substrate for subtilisin Thermus aquaticus N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?

Synonyms

Synonyms Comment Organism
S08.051 Merops ID Thermus aquaticus