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

Abstract

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.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Oak Ridge National Lab., TN (USA)
OSTI Identifier:
6432826
Report Number(s):
CONF-8706127-1
ON: DE87011124
DOE Contract Number:  
AC05-84OR21400
Resource Type:
Conference
Resource Relation:
Conference: Plant molecular biology, Copenhagen, Denmark, 10 Jun 1987
Country of Publication:
United States
Language:
English
Subject:
14 SOLAR ENERGY; 59 BASIC BIOLOGICAL SCIENCES; RIBULOSE DIPHOSPHATE CARBOXYLASE; BIOCHEMICAL REACTION KINETICS; GENE MUTATIONS; STRUCTURE-ACTIVITY RELATIONSHIPS; AMINO ACID SEQUENCE; BIOMIMETIC PROCESSES; SPECIES DIVERSITY; SPINACH; CARBON-CARBON LYASES; CARBOXY-LYASES; ENZYMES; FOOD; KINETICS; LYASES; MOLECULAR STRUCTURE; MUTATIONS; PLANTS; REACTION KINETICS; VEGETABLES; 140505* - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-); 550200 - Biochemistry

Citation Formats

Hartman, F C, Foote, R S, Larimer, F W, Lee, E H, Machanoff, R, Milanez, S, Mitra, S, Mural, R J, Niyogi, S K, and Smith, H B. Function of active-site residues of ribulose bisphosphate carboxylase/oxygenase. United States: N. p., 1987. Web.
Hartman, F C, Foote, R S, Larimer, F W, Lee, E H, Machanoff, R, Milanez, S, Mitra, S, Mural, R J, Niyogi, S K, & Smith, H B. Function of active-site residues of ribulose bisphosphate carboxylase/oxygenase. United States.
Hartman, F C, Foote, R S, Larimer, F W, Lee, E H, Machanoff, R, Milanez, S, Mitra, S, Mural, R J, Niyogi, S K, and Smith, H B. Thu . "Function of active-site residues of ribulose bisphosphate carboxylase/oxygenase". United States.
@article{osti_6432826,
title = {Function of active-site residues of ribulose bisphosphate carboxylase/oxygenase},
author = {Hartman, F C and Foote, R S and Larimer, F W and Lee, E H and Machanoff, R and Milanez, S and Mitra, S and Mural, R J and Niyogi, S K and Smith, H B},
abstractNote = {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.},
doi = {},
url = {https://www.osti.gov/biblio/6432826}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1987},
month = {1}
}

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