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New insight into the pyruvate decarboxylase-catalysed formation of lactaldehyde from H-D exchange experiments: A 'water proof' active site
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UNSPECIFIED (1996) New insight into the pyruvate decarboxylase-catalysed formation of lactaldehyde from H-D exchange experiments: A 'water proof' active site. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1 (13). pp. 1577-1581. ISSN 0300-922X
Full text not available from this repository.Abstract
Pyruvate decarboxylase from Saccharomyces cerevisiae catalyses the formation of lactaldehyde from sodium glyoxylate and acetaldehyde. By using deuteriated sodium glyoxylate (sodium [2-H-2] glyoxylate monohydrate) as a substrate it was verified that the lactaldehyde formed retains the deuterium atom. The implications of the observed result for the enzyme mechanism are discussed in the light of conclusions derived from recent molecular modelling studies.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Journal or Publication Title: | JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 1 |
| Publisher: | ROYAL SOC CHEMISTRY |
| ISSN: | 0300-922X |
| Date: | 7 July 1996 |
| Number: | 13 |
| Number of Pages: | 5 |
| Page Range: | pp. 1577-1581 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/18599 |
Data sourced from Thomson Reuters' Web of Knowledge
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