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Literature summary for 2.4.2.31 extracted from

  • Carpusca, I.; Schirmer, J.; Aktories, K.
    Two-site autoinhibition of the ADP-ribosylating mosquitocidal toxin (MTX) from Bacillus sphaericus by its 70-kDa ricin-like binding domain (2004), Biochemistry, 43, 12009-12019.
    View publication on PubMed
Search for more literature for 2.4.2.31

Inhibitors

Inhibitors Comment Organism Structure
additional information activation of enzyme by proteolytic cleaveage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal fragment. In solution, the fragment is still a potent inhibitor of enzyme activity. Amino acids D273 and D275 are essential for inhibitory effect. Peptide 265-285 increases the Km-value for NAD. Two-site binding model for inhibition Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0403
-
 NAD+ pH 7.4, absence of peptide 265-285 Lysinibacillus sphaericus
1.133
-
 NAD+ pH 7.4, presence of peptide 265-285 Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification activation of enzyme by proteolytic cleavage releasing the active enzyme, amino acids 30-264, and a 70 kDa C-terminal inhibitory fragment Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
soy bean trypsin inhibitor + NAD+
-
 Lysinibacillus sphaericus nicotinamide + ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2
-
 NAD+ pH 7.4, absence of peptide 265-285 Lysinibacillus sphaericus
10.6
-
 NAD+ pH 7.4, presence of peptide 265-285 Lysinibacillus sphaericus