Function of active-site residues of ribulose-bisphosphate carboxylase/oxygenase (Rubisco)

Conference · Sun Jan 01 04:00:00 EST 1989

OSTI ID:5729064

Hartman, F C; Lee, E H; Smith, H B

Chemical modification, site-directed mutagenesis, and x-ray crystallography have identified Lys166, Lys329, and Glu48 as active-site residues of the homodimeric Rubisco from Rhodospirillum rubrum. (In the L/sub 8/S/sub 8/ Rubisco from spinach, these residues correspond to Lys175, Lys334, and Glu60.) We have used two strategies to explore the function of these residues: (a) introduction of very subtle structural changes into their side chains by combining chemical modification with site-directed mutagenesis and (b) evaluation of the ability of mutant proteins, devoid in overall carboxylase activity, to catalyze the enolization of D-ribulose-1,5-bisphosphate (RuBP), i.e. the first step in the normal reaction pathway. 15 refs., 2 figs.

• Research Organization: Oak Ridge National Lab., TN (USA)
• DOE Contract Number: AC05-84OR21400
• OSTI ID: 5729064
• Report Number(s): CONF-8908117-1; ON: DE89016264
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
BACTERIA
BIOCHEMICAL REACTION KINETICS
CARBON-CARBON LYASES
CARBOXY-LYASES
CARBOXYLIC ACIDS
CATALYSIS
ENZYMES
EVALUATION
KINETICS
LYASES
LYSINE
MICROORGANISMS
MOLECULAR STRUCTURE
MUTANTS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
REACTION KINETICS
RHODOSPIRILLUM
RIBULOSE DIPHOSPHATE CARBOXYLASE
STRUCTURE-ACTIVITY RELATIONSHIPS