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Enzyme catalysis: not different, just better
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title
Enzyme catalysis: not different, just better
(English)
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author name string
J R Knowles
series ordinal
1
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language of work or name
English
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publication date
14 March 1991
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published in
Nature
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volume
350
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page(s)
121-4
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issue
6314
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cites work
Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product
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Structure-function relationships in lactate dehydrogenase
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Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis
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THE STRUCTURE OF CARBOXYPEPTIDASE A, IV. PRELIMINARY RESULTS AT 2.8 Å RESOLUTION, AND A SUBSTRATE COMPLEX AT 6 Å RESOLUTION.
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Glucose-induced conformational change in yeast hexokinase
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Structure and activity of phosphoglycerate mutase
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Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data
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On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
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Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis
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Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.
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Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.
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Phosphate-binding sequences in nucleotide-binding proteins
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Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint
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Biological properties of human c-Ha-ras1 genes mutated at codon 12.
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Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli
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NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
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Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
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Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate
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The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase.
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Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
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Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism
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How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases
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15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism.
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The role of the alpha-helix dipole in protein function and structure
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The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of α-helices
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Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain
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Critical ionization states in the reaction catalyzed by triosephosphate isomerase
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7 January 2021
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Enzyme substrate and inhibitor interactions
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Molecular Architecture and Biological Reactions
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Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering
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Einfluss der Configuration auf die Wirkung der Enzyme
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Free-energy profile of the reaction catalyzed by triosephosphate isomerase
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Identifiers
DOI
10.1038/350121A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2136701
Dimensions Publication ID
1040243088
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OpenCitations bibliographic resource ID
2136701
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2136701
PubMed ID
2005961
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2136701
Springer Nature article ID
10.1038/350121a0
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