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The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis

Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme...

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Published in:FEBS letters 2002-05, Vol.518 (1), p.39-42
Main Authors: Kursula, Inari, Partanen, Sanna, Lambeir, Anne-Marie, Wierenga, Rik K.
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description Triosephosphate isomerase (TIM) has a conserved salt bridge 20 Å away from both the active site and the dimer interface. In this study, four salt bridge mutants of Trypanosoma brucei brucei TIM were characterized. The folding and stability of the mutants are impaired compared to the wild-type enzyme. This salt bridge is part of a hydrogen bonding network which tethers the C-terminal β7α7β8α8 unit to the bulk of the protein. In the variants D227N, D227A, and R191S, this network is preserved, as can be deduced from the structure of the R191S variant. In the R191A variant, the side chain at position 191 cannot contribute to this network. Also the catalytic power of this variant is most affected.
doi_str_mv 10.1016/S0014-5793(02)02639-X
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source ScienceDirect Journals; Wiley-Blackwell Read & Publish Collection
subjects Animals
Arginine - genetics
Arginine - physiology
Aspartic Acid - genetics
Aspartic Acid - physiology
Binding Sites
Catalysis
Conserved Sequence
DHAP, dihydroxyacetone phosphate
Enzyme Stability
Folding
GAP, glyceraldehyde-3-phosphate
GuHCl, guanidinium hydrochloride
Hydrogen Bonding
Kinetics
Models, Chemical
Models, Molecular
Mutation
PGA, 2-phosphoglycolate
Protein Folding
Salt bridge
Salts - chemistry
Stability
TIM, triosephosphate isomerase
Triose-Phosphate Isomerase - chemistry
Triose-Phosphate Isomerase - genetics
Triose-Phosphate Isomerase - metabolism
Triosephosphate isomerase
Trypanosoma brucei brucei - enzymology
title The importance of the conserved Arg191–Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
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