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Title: Partial reactions and chemical rescue of site-directed mutants of Rubisco as mechanistic probes

Abstract

Given the current state of knowledge of the reaction pathways catalyzed by D-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the elucidation of the three-dimensional structure of several different forms of the enzyme, sit-directed mutagenesis offers the potential to decipher catalytic roles of active-site residues and to unravel the functional significance of various structural elements. Especially intriguing are intersubunit, electrostatic interactions at the active site between Glu48 and Lys168 of the nonactivated (noncarbamylated) enzyme and between Glu48 and Lys329 of the activated (carbamylated) enzyme. In this paper, we describe two approaches to address the roles of electrostatic interactions at the active site and the roles of the participant residues: (1) characterization of pertinent site-directed mutants, including their abilities to catalyze partial reactions and (2) subtle alteration of the active-site microenvironment by manipulation of these proteins with exogenous reagents.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Oak Ridge National Lab., TN (United States)
Sponsoring Org.:
USDOE, Washington, DC (United States)
OSTI Identifier:
10133608
Report Number(s):
CONF-911295-1
ON: DE92007255
DOE Contract Number:  
AC05-84OR21400
Resource Type:
Conference
Resource Relation:
Conference: Royal Swedish Academy of Science (RSAS) nobel symposium,Stockholm (Sweden),4-6 Dec 1991; Other Information: PBD: [1991]
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; PROTEINS; CONFIGURATION INTERACTION; CATALYSTS; PROTEIN ENGINEERING; MUTAGENESIS; REACTION INTERMEDIATES; CATALYSIS; GLUTAMINE; LYSINE; PROTEIN STRUCTURE; CARBOXYLATION; OXYGENASES; ENZYME ACTIVITY; 400201; 550200; CHEMICAL AND PHYSICOCHEMICAL PROPERTIES; BIOCHEMISTRY

Citation Formats

Harpel, M R, Larimer, F W, Lee, E H, Mural, R J, Smith, H B, Soper, T S, and Hartman, F C. Partial reactions and chemical rescue of site-directed mutants of Rubisco as mechanistic probes. United States: N. p., 1991. Web.
Harpel, M R, Larimer, F W, Lee, E H, Mural, R J, Smith, H B, Soper, T S, & Hartman, F C. Partial reactions and chemical rescue of site-directed mutants of Rubisco as mechanistic probes. United States.
Harpel, M R, Larimer, F W, Lee, E H, Mural, R J, Smith, H B, Soper, T S, and Hartman, F C. Tue . "Partial reactions and chemical rescue of site-directed mutants of Rubisco as mechanistic probes". United States.
@article{osti_10133608,
title = {Partial reactions and chemical rescue of site-directed mutants of Rubisco as mechanistic probes},
author = {Harpel, M R and Larimer, F W and Lee, E H and Mural, R J and Smith, H B and Soper, T S and Hartman, F C},
abstractNote = {Given the current state of knowledge of the reaction pathways catalyzed by D-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the elucidation of the three-dimensional structure of several different forms of the enzyme, sit-directed mutagenesis offers the potential to decipher catalytic roles of active-site residues and to unravel the functional significance of various structural elements. Especially intriguing are intersubunit, electrostatic interactions at the active site between Glu48 and Lys168 of the nonactivated (noncarbamylated) enzyme and between Glu48 and Lys329 of the activated (carbamylated) enzyme. In this paper, we describe two approaches to address the roles of electrostatic interactions at the active site and the roles of the participant residues: (1) characterization of pertinent site-directed mutants, including their abilities to catalyze partial reactions and (2) subtle alteration of the active-site microenvironment by manipulation of these proteins with exogenous reagents.},
doi = {},
url = {https://www.osti.gov/biblio/10133608}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1991},
month = {12}
}

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