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

Abstract

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.

Authors:
; ;
Publication Date:
Research Org.:
Oak Ridge National Lab., TN (USA)
OSTI Identifier:
5729064
Report Number(s):
CONF-8908117-1
ON: DE89016264
DOE Contract Number:  
AC05-84OR21400
Resource Type:
Conference
Resource Relation:
Conference: 8. international congress on photosynthesis, Stockholm, Sweden, 6-11 Aug 1989; Other Information: Portions of this document are illegible in microfiche products
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; MOLECULAR STRUCTURE; EVALUATION; PROTEINS; AMINO ACID SEQUENCE; RHODOSPIRILLUM; MUTANTS; BIOCHEMICAL REACTION KINETICS; CATALYSIS; LYSINE; RIBULOSE DIPHOSPHATE CARBOXYLASE; STRUCTURE-ACTIVITY RELATIONSHIPS; AMINO ACIDS; BACTERIA; CARBON-CARBON LYASES; CARBOXY-LYASES; CARBOXYLIC ACIDS; ENZYMES; KINETICS; LYASES; MICROORGANISMS; ORGANIC ACIDS; ORGANIC COMPOUNDS; REACTION KINETICS; 550200* - Biochemistry

Citation Formats

Hartman, F C, Lee, E H, and Smith, H B. Function of active-site residues of ribulose-bisphosphate carboxylase/oxygenase (Rubisco). United States: N. p., 1989. Web.
Hartman, F C, Lee, E H, & Smith, H B. Function of active-site residues of ribulose-bisphosphate carboxylase/oxygenase (Rubisco). United States.
Hartman, F C, Lee, E H, and Smith, H B. Sun . "Function of active-site residues of ribulose-bisphosphate carboxylase/oxygenase (Rubisco)". United States.
@article{osti_5729064,
title = {Function of active-site residues of ribulose-bisphosphate carboxylase/oxygenase (Rubisco)},
author = {Hartman, F C and Lee, E H and Smith, H B},
abstractNote = {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.},
doi = {},
url = {https://www.osti.gov/biblio/5729064}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1989},
month = {1}
}

Conference:
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