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Function of active-site residues of ribulose bisphosphate carboxylase/oxygenase

Conference ·
OSTI ID:6432826
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As one facet of elucidating the mechanism of ribulose-P/sub 2/ carboxylase and of ultimately evaluating the feasibility of altering the carboxylase/oxygenase ratio, active-site characterization has received considerable attention. Chemical modification has revealed five disparate segments of primary structure that appear to constitute the active site. The amino acid sequence of each segment is highly conserved among evolutionarily diverse carboxylases. Site-directed mutagenesis has been used to clarify further the functions of Lys-166, Lys-329, His-291, and Glu-48 of ribulose-P/sub 2/ carboxylase from Rhodospirillum rubrum. These two lysines were selected for examination because of the wealth of data discussed earlier that had implicated their catalytic involvement. His-291 was scrutinized because of the suggestion of its participation, rather than Lys-166, as the proton transfer group that enolizes ribulose-P/sub 2/. The reasons for inspecting Glu-48 were circumstantial. Within the homologous region flanked by His-44 and Cys-58, targets of an affinity label, Glu-48 is the only acid/base group and hence a logical candidate for functionality. Furthermore, crystallographic and chemical cross-linking studies had placed this NH/sub 2/-terminal region near the active site. 33 refs.
Research Organization:
Oak Ridge National Lab., TN (USA)
DOE Contract Number:
AC05-84OR21400
OSTI ID:
6432826
Report Number(s):
CONF-8706127-1; ON: DE87011124
Country of Publication:
United States
Language:
English

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Related Subjects

14 SOLAR ENERGY
140505* -- Solar Energy Conversion-- Photochemical
Photobiological
& Thermochemical Conversion-- (1980-)
550200 -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
BIOCHEMICAL REACTION KINETICS
BIOMIMETIC PROCESSES
CARBON-CARBON LYASES
CARBOXY-LYASES
ENZYMES
FOOD
GENE MUTATIONS
KINETICS
LYASES
MOLECULAR STRUCTURE
MUTATIONS
PLANTS
REACTION KINETICS
RIBULOSE DIPHOSPHATE CARBOXYLASE
SPECIES DIVERSITY
SPINACH
STRUCTURE-ACTIVITY RELATIONSHIPS
VEGETABLES