Ribulosebisphosphate carboxylase/oxygenase: active-site characterization and partial sequence determination
Conference
·
OSTI ID:5060224
Chemical approaches that have been applied to active-site characterization of ribulosebisphosphate carboxylase/oxygenase are reviewed. These include modification with group-specific reagents, affinity labeling, and paracatalytic modification. In an attempt to obtain reagents with a greater specificity for the enzyme's active site, two reactive derivatives (the acid azide and the 3-chloroacetyl compound) of the transition state analog 2-carboxyarabinitol 1,5-bisphosphate have been prepared. The elucidation of the primary structure of the carboxylase/oxygenase from Rhodospirillum rubrum has also been initiated. Tryptic peptides accounting for the enzyme's five sulfhydryl groups and collectively representing twenty percent of the total polypeptide chain have been sequenced. Eight major fragments resulting from cleavage of the enzyme with cyanogen bromide and representing about seventy percent of the total polypeptide chain have been purified for subsequent sequence analyses. A striking observation is the lack of detectable homology between the R. rubrum and barley enzymes based on the limited sequence data currently available.
- Research Organization:
- Oak Ridge National Lab., TN (USA); Tennessee Univ., Oak Ridge (USA). Graduate School of Biomedical Sciences
- DOE Contract Number:
- W-7405-ENG-26
- OSTI ID:
- 5060224
- Report Number(s):
- CONF-800963-1
- Country of Publication:
- United States
- Language:
- English
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