Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation (Q27734472)

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English	Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation	scientific article

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Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation (English)

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author name string

B E Bernstein

1

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P A Michels

2

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W G Hol

3

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language of work or name

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publication date

16 January 1997

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385

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6613

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275-8

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Structure of horse muscle phosphoglycerate kinase. Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 angstrom Fourier map.

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Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate

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Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate

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Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme

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Enzyme-Catalyzed Phosphoryl Transfer Reactions

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Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products

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Compartmentation of carbohydrate metabolism in trypanosomes

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A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement

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Solvent content of protein crystals

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AMoRe: an automated package for molecular replacement

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The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies

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Site-directed mutagenesis of yeast phosphoglycerate kinase. The 'basic-patch' residue arginine 168.

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Characterization of the structure and properties of the His 62 → Ala and Arg 38 → Ala mutants of yeast phosphoglycerate kinase: An investigation of the catalytic and activatory sites by site‐directed mutagenesis and NMR

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10.1038/385275A0

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