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Tello, Mónica, Rejzek, Martin, Wilkinson, Barrie, Lawson, David M. and Field, Robert A. 
ORCID: https://orcid.org/0000-0001-8574-0275
(2008)
Tyl1a, a TDP-6-deoxy-D-xylo-4-hexulose 3, 4-isomerase from Streptomyces fradiae:Structure prediction, mutagenesis and solvent isotope incorporation experiments to investigate reaction mechanism.
ChemBioChem, 9 (8).
pp. 1295-1302.
ISSN 1439-4227
Abstract
Understanding the structure and mechanism of sugar nucleotide processing enzymes is invaluable in the generation of designer enzymes for biotransformation, for instance, in connection with engineering antibiotic glycosylation. In this study, homology modelling and mechanistic comparison to the structurally related RmlC epimerase family has been used to identify and assign functions to active-site residues in the Tyl1a-catalysed keto-sugar nucleotide isomerisation process. Tyl1a His63 is implicated as the base that initiates the isomerisation process by substrate C-3 deprotonation, with Arg109 stabilising the resulting enolate. Subsequent O-3 deprotonation (potentially by His65) and C-4 protonation (potentially by Tyr49) complete the isomerisation process.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | antibiotics,enzyme catalysis,isomerases,structure analysis,sugar nucleotides,biochemistry,molecular medicine,molecular biology,organic chemistry ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009) |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 06 Sep 2024 13:35 |
| Last Modified: | 25 Sep 2024 18:07 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96605 |
| DOI: | 10.1002/cbic.200800021 |
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