Effect of conformation of the substrate on enzymatic eecarboxylation of α-Arylmalonic Acid
- 1 June 1994
- journal article
- research article
- Published by Elsevier in Bioorganic & Medicinal Chemistry
- Vol. 2 (6) , 469-475
- https://doi.org/10.1016/0968-0896(94)80016-2
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Purification and properties of a novel arylmalonate decarboxylase from Alcaligenes bronchisepticus KU 1201European Journal of Biochemistry, 1992
- Microbial asymmetric decarboxylation of fluorine-containing arylmalonic acid derivativesJournal of Fluorine Chemistry, 1992
- A fifth-order method for two-electron integral derivative transformationChemical Physics Letters, 1992
- Asymmetric Decarboxylation of Disubstituted Malonic Acid by Alcaligenes bronchisepticus KU 1201Biocatalysis, 1991
- Enzymes in organic synthesis. 47. Active-site model for interpreting and predicting the specificity of pig liver esteraseJournal of the American Chemical Society, 1990
- Enzyme-mediated asymmetric decarboxylation of disubstituted malonic acidsJournal of the American Chemical Society, 1990
- A new cubic-space section model for predicting the specificity of horse liver alcohol dehydrogenase-catalyzed oxidoreductionsCanadian Journal of Chemistry, 1982
- The Darzens glycidic ester condensation of indan-1-ones. A reinvestigation of the reactionCanadian Journal of Chemistry, 1978
- Mandelic acid racemase from Pseudomonas putida. Evidence favoring a carbanion intermediate in the mechanism of actionBiochemistry, 1970
- Mandelic acid racemase from Pseudomonas putida. Purification and properties of the enzymeBiochemistry, 1970