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Literature summary for 3.4.24.69 extracted from

  • Ahmed, S.A.; Byrne, M.P.; Jensen, M.; Hines, H.B.; Brueggemann, E.; Smith, L.A.
    Enzymatic autocatalysis of botulinum A neurotoxin light chain (2001), J. Protein Chem., 20, 221-231.
    View publication on PubMed
Search for more literature for 3.4.24.69

Cloned(Commentary)

Cloned (Comment) Organism
-
 Clostridium botulinum

Inhibitors

Inhibitors Comment Organism Structure
CRATKML competitive peptide inhibitor Clostridium botulinum

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc endopeptidase, Zn2+ is the natural cofactor of the light chain Clostridium botulinum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Clostridium botulinum undergoes autocatalytic proteolytic processing and fragmentation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium botulinum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information undergoes autocatalytic proteolytic processing and fragmentation Clostridium botulinum ?
-
 ?
SNAP-25 + H2O
-
 Clostridium botulinum ?
-
 ?

Synonyms

Synonyms Comment Organism
BoNT
-
 Clostridium botulinum
botulinum A neurotoxin light chain
-
 Clostridium botulinum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.002
-
 CRATKML pH 6.5, 22°C Clostridium botulinum