The form of 2-phosphoglycollic acid bound by triosephosphate isomerase. |
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| Authors: | I D Campbell R B Jones P A Kiener E Richards S C Waley R Wolfenden |
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| Affiliation: | 1. Department of Biochemistry, University of Oxford, Oxford, England.;2. Sir William Dunn School of Pathology, University of Oxford, Oxford, England.;3. Dyson Perrins Laboratory, University of Oxford, Oxford, England.;4. Department of Biochemistry, University of North Carolina, Chapel Hill, North Carolina 27514 USA |
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| Abstract: | In NMR experiments designed to distinguish between possible enzyme-bound forms of the inhibitor 2-phosphoglycollic acid, it is found that neither of the di-anionic species, that would be consistent with the observed pH-dependence of Ki, is in fact correct. Instead, the enzyme appears to bind the tri-anionic species of this inhibitor, taking up a proton at a separate site. |
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| Keywords: | to which inquiries should be addressed. |
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