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PubMed · 15271345

Cellular addresses; step one in creating a glycocode.

Nicola Pohl
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Abstract

In this issue of Chemistry & Biology, a library screening approach reveals at least four types of enzymes that attach galactosamine to build cell surface mucin-type glycoproteins. A better molecular understanding of how these information-carrying oligosaccharides are created sets the stage for designing more selective inhibitors and potential therapeutics.

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Nicola Pohl. 2004. Cellular addresses; step one in creating a glycocode.. https://doi.org/10.1016/j.chembiol.2004.07.004

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Alpha-secondary isotope effects as probes of "tunneling-ready" configurations in enzymatic H-tunneling: insight from environmentally coupled tunneling models.

Using alpha-secondary kinetic isotope effects (2 degrees KIEs) in conjunction with primary (1 degrees ) KIEs, we have investigated the mechanism of environmentally coupled hydrogen tunneling in the reductive half-reactions of two homologous flavoenzymes, morphinone reductase (MR) and pentaerythritol tetranitrate reductase (PETNR). We find exalted 2 degrees KIEs (1.17-1.18) for both enzymes, consistent with hydrogen tunneling. These 2 degrees KIEs, unlike 1 degrees KIEs, are independent of promoting motions-a nonequilibrium pre-organization of cofactor and active site residues that is required to bring the reactants into a "tunneling-ready" configuration. That these 2 degrees KIEs are identical suggests the geometries of the "tunneling-ready" configurations in both enzymes are indistinguishable, despite the fact that MR, but not PETNR, has a clearly temperature-dependent 1 degrees KIE. The work emphasizes the benefit of combining studies of 1 degrees and 2 degrees KIEs to report on pre-organization and local geometries within the context of contemporary environmentally coupled frameworks for H-tunneling.

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