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- Cameron, AD, et al.
(author)
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Crystal structure of human glyoxalase .1. Evidence for gene duplication and 3D domain swapping
- 1997
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In: EMBO JOURNAL. - : OXFORD UNIV PRESS. - 0261-4189. ; 16:12, s. 3386-3395
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Journal article (other academic/artistic)abstract
- The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and r
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| 3. |
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| 4. |
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| 5. |
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| 6. |
- Mannervik, B, et al.
(author)
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An evolutionary approach to the design of glutathione-linked enzymes
- 1998
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In: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 112, s. 15-21
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Journal article (other academic/artistic)abstract
- Studies of protein structure provide information about principles of protein design that have come into play in natural evolution. This information can be exploited in the redesign of enzymes for novel functions. The glutathione-binding domain of glutathi
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| 7. |
- Mowbray, SL, et al.
(author)
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Errors and reproducibility in electron-density map interpretation
- 1999
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In: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. - : MUNKSGAARD INT PUBL LTD. - 0907-4449. ; 55, s. 1309-1319
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Journal article (other academic/artistic)abstract
- Three investigators, with varying levels of experience, independently built and refined the structure of Escherichia coli ribokinase at 2.6 Angstrom resolution. At the end of the refinement/rebuilding processes the models had essentially converged, althou
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| 8. |
- Ridderstrom, M, et al.
(author)
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Involvement of an active-site Zn2+ ligand mechanism of human glyoxalase I
- 1998
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In: JOURNAL OF BIOLOGICAL CHEMISTRY. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258. ; 273:34, s. 21623-21628
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Journal article (other academic/artistic)abstract
- The Zn2+ ligands glutamate 99 and glutamate 172 in the active site of human glyoxalase I were replaced, each in turn, by glutamines by site-directed mutagenesis to elucidate their potential significance for the catalytic properties of the enzyme. To compe
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| 9. |
- Ridderstrom, M, et al.
(author)
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Mutagenesis of residue 157 in the active site of human glyoxalase I
- 1997
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In: BIOCHEMICAL JOURNAL. - : PORTLAND PRESS. - 0264-6021. ; 328, s. 231-235
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Journal article (other academic/artistic)abstract
- Met-157 in the active site of human glyoxalase I was changed by site-directed mutagenesis into alanine, glutamine or histidine in order to evaluate its possible role in catalysis. The glyoxalase I mutants were expressed in Escherichia coli and purified on
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| 10. |
- Sigrell, JA, et al.
(author)
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Induced fit on sugar binding activates ribokinase
- 1999
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In: JOURNAL OF MOLECULAR BIOLOGY. - : ACADEMIC PRESS LTD. - 0022-2836. ; 290:5, s. 1009-1018
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Journal article (other academic/artistic)abstract
- The enzyme ribokinase phosphorylates ribose at O5* as the first step in its metabolism. The original X-ray structure of Escherichia coli ribokinase represented the ternary complex including ribose and ADP. Structures are presented here for the apo enzyme,
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