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. 1991 May;96(1):335–339. doi: 10.1104/pp.96.1.335

Protection of Tryptic-Sensitive Sites in the Large Subunit of Ribulosebisphosphate Carboxylase/Oxygenase by Catalysis 1

Robert L Houtz 1,2, R Michael Mulligan 1,2
PMCID: PMC1080758  PMID: 16668178

Abstract

Limited tryptic proteolysis of spinach (Spinacia oleracea) ribulose bisphosphate carboxylase/oxygenase (ribulose-P2 carboxylase) resulted in the ordered release of two adjacent N-terminal peptides from the large subunit, and an irreversible, partial inactivation of catalysis. The two peptides were identified as the N-terminal tryptic peptide (acetylated Pro-3 to Lys-8) and the penultimate tryptic peptide (Ala-9 to Lys-14). Kinetic comparison of hydrolysis at Lys-8 and Lys-14, enzyme inactivation, and changes in the molecular weight of the large subunit, indicated that proteolysis at Lys-14 correlated with inactivation, while proteolysis at Lys-8 occurred much more rapidly. Thus, enzyme inactivation is primarily the result of proteolysis at Lys-14. Proteolysis of ribulose-P2 carboxylase under catalytic conditions (in the presence of CO2, Mg2+, and ribulose-P2) also resulted in ordered release of these tryptic peptides; however, the rate of proteolysis at lysyl residues 8 and 14 was reduced to approximately one-third of the rate of proteolysis of these lysyl residues under noncatalytic conditions (in the presence of CO2 and Mg2+ only). The protection of these lysyl residues from proteolysis under catalytic conditions could reflect conformational changes in the N-terminal domain of the large subunit which occur during the catalytic cycle.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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