13C NMR as a probe for the study of enzyme‐catalysed reactions
- 2 June 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 114 (2) , 283-286
- https://doi.org/10.1016/0014-5793(80)81134-3
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Mechanism of action of 5-aminolevulinic acid dehydratese: stepwise order of addition of the two molecules of 5-aminolevulinic acid in the enzymic synthesis of porphobilinogenJournal of the Chemical Society, Chemical Communications, 1980
- The biosynthesis of uroporphyrinogen III: Order of assembly of the four porphobilinogen molecules in the formation of the tetrapyrrole ringFEBS Letters, 1979
- 13C n.m.r. evidence for a new intermediate, pre-uroporphyrinogen, in the enzymic transformation of porphobilinogen into uroporphyrinogens I and IIIJournal of the Chemical Society, Chemical Communications, 1979
- Pre-uroporphyrinogen: a substrate for uroporphyrinogen III cosynthetaseJournal of the Chemical Society, Chemical Communications, 1979
- Direct observation of porphyrinogen biosynthesis in living cells by 13C n.m.r. spectroscopyJournal of the Chemical Society, Chemical Communications, 1979
- High-resolution 13C nuclear magnetic resonance studies of glucose metabolism in Escherichia coli.Proceedings of the National Academy of Sciences, 1978
- Evidence for hemiacetal formation between α-chymotrypsin and hydrocinnamaldehyde by cross-saturation nuclear magnetic resonance spectroscopyJournal of the Chemical Society, Chemical Communications, 1977
- 5-Aminolaevulinic acid dehydratase: structure, function, and mechanismPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1976
- Biosynthesis of porphyrins and corrinsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1976
- Carbon-13 as a Label in Biosynthetic StudiesScience, 1974