Zobrazeno 1 - 10 of 12 pro vyhledávání: '"C A, Collyer"'
1
Arthrobacter d-xylose isomerase: protein-engineered subunit interfaces
Autor: J. D. Goldberg, M Rangarajan, L Varsani, Brian S. Hartley, C. A. Collyer, David M. Blow, T Cui
Publikováno v: Biochemical Journal. 291:575-583
Mutants of Arthrobacter D-xylose isomerase were constructed in which one or two disulphide bridges or additional salt bridges were introduced at the A-A* subunit interfaces. These showed no change in enzyme activity or stability compared with the wil
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b85321bd4edaf347a39f55256fadc4a
https://doi.org/10.1042/bj2910575
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2
Conventional X-ray diffraction approaches to the study of enzyme mechanism: serine proteinases, aminoacyl-tRNA synthetases and xylose isomerase
Autor: O. Smart, C. A. Collyer, Peter Brick, J. D. Goldberg, David M. Blow
Publikováno v: Philosophical Transactions of the Royal Society of London. Series A: Physical and Engineering Sciences. 340:311-321
Techniques that have been used to study enzyme mechanism by conventional steady-state crystallographic techniques are reviewed. Substrates and substrate analogues can often be diffused into crystals, but occasionally co-crystallization is necessary.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b0a01262c200975c345521bc6acde3c9
https://doi.org/10.1098/rsta.1992.0069
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3
Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase
Autor: C A Collyer, D M Blow
Publikováno v: Proceedings of the National Academy of Sciences. 87:1362-1366
Crystallographic studies of D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) incubated to equilibrium with substrate/product mixtures of xylose and xylulose show electron density for a bound intermediate. The accumulation of this bound inter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c48ef2c6dd1b3bce31126019e36a4389
https://doi.org/10.1073/pnas.87.4.1362
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5
Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism
Autor: D B, Langley, M D, Templeton, B A, Fields, R E, Mitchell, C A, Collyer
Publikováno v: The Journal of biological chemistry. 275(26)
The crystal structure is reported at 1.8 A resolution of Escherichia coli ornithine transcarbamoylase in complex with the active derivative of phaseolotoxin from Pseudomonas syringae pv. phaseolicola, N(delta)-(N'-sulfodiaminophosphinyl)-l-ornithine.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::91c5b2f9f27b8d9f09ef7c932592f251
https://pubmed.ncbi.nlm.nih.gov/10747936
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6
Trigonal crystals of glucose isomerase require thymol for their growth and stability
Autor: David M. Blow, Lesley F. Lloyd, Naomi E. Chayen, C. A. Collyer
Publikováno v: Journal of Crystal Growth. 97:367-374
The growth of trigonal bypyramidal crystals of Arthrobacter glucose isomerase is only possible in the presence of thymol at a concentration exceeding 2.5mM; at lower thymol concentrations rectangular and rhombic crystals are formed. When thymol is re
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4925b2a87c77b0b99feaff82fa03217c
https://doi.org/10.1016/0022-0248(89)90218-2
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