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Literature summary for 5.5.1.6 extracted from

  • Terai, Y.; Fujii, I.; Byun, S.H.; Nakajima, O.; Hakamatsuka, T.; Ebizuka, Y.; Sankawa, U.
    Cloning of chalcone-flavanone isomerase cDNA from Pueraria lobata and its overexpression in Escherichia coli (1996), Protein Expr. Purif., 8, 183-190.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Pueraria montana var. lobata

Protein Variants

Protein Variants Comment Organism
C119A mutant enzyme Cys119Ala, is less sensitive to SH-inhibitors, shows chalcone isomerase activity Pueraria montana var. lobata

Inhibitors

Inhibitors Comment Organism Structure
HgCl2 mutant enzyme Cys119Ala, is less sensitive than wild type enzyme Pueraria montana var. lobata
iodoacetamide mutant enzyme Cys119Ala, is less sensitive than wild type enzyme Pueraria montana var. lobata
NEM mutant enzyme Cys119Ala, is less sensitive than wild type enzyme Pueraria montana var. lobata

Organism

Organism UniProt Comment Textmining
Pueraria montana var. lobata Q43056
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Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pueraria montana var. lobata

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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Pueraria montana var. lobata