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Literature summary for 4.1.1.39 extracted from

  • Li, S.; Lu, W.; Li, G.F.; Gong, Y.D.; Zhao, N.M.; Zhang, R.X.; Zhou, H.M.
    Interaction of hydrogen peroxide with ribulose-1,5-bisphosphate carboxylase/oxygenase from rice (2004), Biochemistry (Moscow), 69, 1136-1142.
    View publication on PubMed

General Stability

General Stability Organism
at low H2O2 concentrations (0.2-10 mM), the properties of the enzyme (e.g., structure and susceptibility to heat denaturation) change slightly. At higher H2O2 concentrations (10-200 mM), rubisco undergoes an unfolding process, including the loss of secondary and tertiary structure, forming extended hydrophobic interface, and leading to cross links between large subunits. High concentrations of H2O2 can also result in an increase in susceptibility of rubisco to heat denaturation. Further pretreatments with or without reductive reagents to rubisco show that the disulfide bonds in rubisco help to protect the enzyme from damage by H2O2 as well as other reactive oxygen species Oryza sativa

Organism

Organism UniProt Comment Textmining
Oryza sativa
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-
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Synonyms

Synonyms Comment Organism
Rubisco
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Oryza sativa