The active site of ribulose-bisphosphate carboxylase/oxygenase

Conference · Tue Jan 01 04:00:00 EST 1991

OSTI ID:6074751

Hartman, F C

The active site of ribulose-bisphosphate carboxylase/oxygenase requires interacting domains of adjacent, identical subunits. Most active-site residues are located within the loop regions of an eight-stranded {beta}/{alpha}-barrel which constitutes the larger C-terminal domain; additional key residues are located within a segment of the smaller N-terminal domain which partially covers the mouth of the barrel. Site-directed mutagenesis of the gene encoding the enzyme from Rhodospirillum rubrum has been used to delineate functions of active-site residues. 6 refs., 2 figs.

• Research Organization: Oak Ridge National Lab., TN (USA)
• Sponsoring Organization: DOE/ER
• DOE Contract Number: AC05-84OR21400
• OSTI ID: 6074751
• Report Number(s): CONF-910161-1; ON: DE91005903
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BACTERIA
CARBOHYDRATES
CARBON CYCLE
CARBON DIOXIDE FIXATION
CARBON-CARBON LYASES
CARBOXY-LYASES
CARBOXYLASE
CHEMICAL REACTIONS
COHERENT SCATTERING
CRYSTALLOGRAPHY
DIFFRACTION
ENZYME ACTIVITY
ENZYMES
KETONES
LYASES
MICROORGANISMS
MONOSACCHARIDES
MUTAGENESIS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
OXYGENASES
PENTOSES
PHOTOCHEMICAL REACTIONS
PHOTOSYNTHESIS
PROTEIN ENGINEERING
RHODOSPIRILLUM
RIBULOSE
RIBULOSE DIPHOSPHATE CARBOXYLASE
SACCHARIDES
SCATTERING
STRUCTURE-ACTIVITY RELATIONSHIPS
SUBSTRATES
SYNTHESIS
X-RAY DIFFRACTION