Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase. The question of nonproductive binding of the substrate hydrate-Reference-Cited by-同舟云学术

Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase. The question of nonproductive binding of the substrate hydrate

Published:1977-06-14 Issue:12 Volume:16 Page:2738-2741
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Webb Martin R.,Standring David N.,Knowles Jeremy R.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00631a023

Reference15 articles.

1. Free-energy profile for the reaction catalyzed by triosephosphate isomerase

2. Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine

3. 31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase

4. Examination of D-fructose 1,6-diphosphate and related sugar phosphates by Fourier transform phosphorus-31 nuclear magnetic resonance spectroscopy

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