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Literature summary for 5.2.1.8 extracted from

  • Goethel, S.F.; Scholz, C.; Schmid, F.X.; Marahiel, M.A.
    Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions (1998), Biochemistry, 37, 13392-13399.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
lactalbumin reduced and carboxymethylated, strong inhibition by the permanently unfolded protein Bacillus subtilis
RNase T1 reduced and carboxymethylated form of the P39A variant, strong inhibition by the permanently unfolded protein Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00045
-
RNase T1 trigger factor Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17600
-
cyclophilin Bacillus subtilis
47300
-
trigger factor Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity. The prolyl isomerases become essential for growth under starvation conditions ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity Bacillus subtilis ?
-
?
additional information only two enzymes, the cyclophilin and the trigger factor, contribute to the peptidylprolyl isomerase activity. The prolyl isomerases become essential for growth under starvation conditions Bacillus subtilis ?
-
?
RNAse T1 reduced and carboxymethylated form of the S54G/P55N variant of RNAse T1. In the native state the Rnase T1 contains a single prolyl bond Tyr38-Pro39. Of all reduced and carboxymethylated RNAse T1 molecules, 85% fold in a monophasic and reversible reaction, which is limited in rate by the slow trans to cis isomerization at Pro39 Bacillus subtilis ?
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
-
Bacillus subtilis succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
?

Synonyms

Synonyms Comment Organism
Cyclophilin
-
Bacillus subtilis
trigger factor
-
Bacillus subtilis