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Literature summary for 5.2.1.8 extracted from

  • Hu, K.; Galius, V.; Pervushin, K.
    Structural plasticity of peptidyl-prolyl isomerase sFkpA is a key to its chaperone function as revealed by solution NMR (2006), Biochemistry, 45, 11983-11991.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
NMR-study of enzyme and its complexes with substrates RNase A and reduced carboxymethylated bovine alpha-lactalbumin in solution. Molecular model of chaperone activity of enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P45523
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced carboxymethylated bovine alpha-lactalbumin
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Escherichia coli reduced carboxymethylated bovine alpha-lactalbumin
-
?
RNase A S-protein partially folded Escherichia coli RNase A S-protein action of enzyme greatly reduces the population of aggregated oligomeric species ?

Synonyms

Synonyms Comment Organism
sFkpA
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Escherichia coli