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Volume 93, 1992
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Structure and mechanism of D-xylose isomerase


The action of xylose isomerase depends on the presence of two divalent cations. Crystal structure analyses of the free enzyme, and of the enzyme bound to a variety of substrates and inhibitors, have provided models for a number of distinct intermediates along the reaction pathway. These models, in turn, have suggested detailed mechanisms for the various chemical steps of the reaction: a ring opening catalysed by an activated histidine, a hydride-shift isomerization, and a ring closure which may be facilitated by a polarised water molecule.

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Article type: Paper
DOI: 10.1039/FD9929300067
Citation: Faraday Discuss., 1992,93, 67-73
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    Structure and mechanism of D-xylose isomerase

    D. M. Blow, C. A. Collyer, J. D. Goldberg and O. S. Smart, Faraday Discuss., 1992, 93, 67
    DOI: 10.1039/FD9929300067

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