Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 44, Issue -, Pages 51-60Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20150177
Keywords
ab initio molecular dynamics; enzyme catalysis; glycosyltransferases; metadynamics; quantum mechanics/molecular mechanics; retention of configuration
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Funding
- Generalitat de Catalunya [2014SGR-987]
- Ministerio de Economia y Competitividad [CTQ2014-55174-P]
- ICREA Funding Source: Custom
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The catalytic mechanism of retaining glycosyltransferases (ret-GTs) remains a controversial issue in glycobiology. By analogy to the well-established mechanism of retaining glycosidases, it was first suggested that ret-GTs follow a double-displacement mechanism. However, only family 6 GTs exhibit a putative nucleophile protein residue properly located in the active site to participate in catalysis, prompting some authors to suggest an unusual single-displacement mechanism [named as front-face or S(N)i (substitution nucleophilic internal)-like]. This mechanism has now received strong support, from both experiment and theory, for several GT families except family 6, for which a double-displacement reaction is predicted. In the last few years, we have uncovered the molecular mechanisms of several retaining GTs by means of quantum mechanics/molecular mechanics (QM/MM) metadynamics simulations, which we overview in the present work.
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