Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product

scientific article published on December 14, 1976

Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/BI00670A027
P698PubMed publication ID999834

P2093author name stringJ. R. Knowles
W. J. Albery
S. G. Maister
C. P. Pett
P433issue25
P407language of work or nameEnglishQ1860
P1104number of pages6
P304page(s)5607-5612
P577publication date1976-12-01
1976-12-14
P1433published inBiochemistryQ764876
P1476titleEnergetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in product
P478volume15

Reverse relations

cites work (P2860)
Q39163528Apparent equivalence of the active-site glutamyl residue and the essential group with pKa 6.0 in triosephosphate isomerase
Q41335123Characterization of stress and methylglyoxal inducible triose phosphate isomerase (OscTPI) from rice
Q28269755Enzyme catalysis: not different, just better
Q39719852Kinetic Isotope Effects in Enzymology
Q90381590Limitations of Deuterium-Labelled Substrates for Quantifying NADPH Metabolism in Heterotrophic Arabidopsis Cell Cultures
Q39158326Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: Phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties
Q40088886Phosphoglycerate mutase from wheat germ: studies with oxygen-18-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediate
Q41984315Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl-CoA in tritiated water
Q35629593Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.
Q35901179The mechanism of rate-limiting motions in enzyme function.
Q31043969Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion.

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