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International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 8(68), p. 1019-1029, 2012

DOI: 10.1107/s0907444912019592

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Structural and biochemical characterization of a trapped coenzyme A adduct ofCaenorhabditis elegansglucosamine-6-phosphateN-acetyltransferase 1

Journal article published in 2012 by Helge C. Dorfmueller ORCID, Wenxia Fang, Francesco V. Rao, David E. Blair, Helen Attrill, Daan M. F. van Aalten ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Glucosamine-6-phosphate N-acetyltransferase 1 (GNA1) produces GlcNAc-6-phosphate from GlcN-6-phosphate and acetyl coenzyme A. Early mercury-labelling experiments implicated a conserved cysteine in the reaction mechanism, whereas recent structural data appear to support a mechanism in which this cysteine plays no role. Here, two crystal structures of Caenorhabditis elegans GNA1 are reported, revealing an unusual covalent complex between this cysteine and the coenzyme A product. Mass-spectrometric and reduction studies showed that this inactive covalent complex can be reactivated through reduction, yet mutagenesis of the cysteine supports a previously reported bi-bi mechanism. The data unify the apparently contradictory earlier reports on the role of a cysteine in the GNA1 active site. ©2012 International Union of Crystallography.