Inhibition of d-xylose isomerase by pentitols and d-lyxose
Identifieur interne : 000216 ( 1968/Analysis ); précédent : 000215; suivant : 000217Inhibition of d-xylose isomerase by pentitols and d-lyxose
Auteurs : Kei Yamanaka [Japon]Source :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1969.
English descriptors
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Abstract
Abstract: The inhibition of crystalline d-xylose isomerase from Lactobacillus brevis by pentitols and carbohydrate derivatives has been examined. Of the pentitols, xylitol and l- and d-arabitol inhibited competitively, whereas ribitol was ineffective. The inhibition constants (Ki) are: 0.0027, 0.13, or 0.146 m for xylitol, d-arabitol, and l-arabitol, respectively. d-Lyxose also inhibited competitively with a Ki of 0.07 m. The kinetic data indicate that the substrate, d-xylose, and these inhibitors combine at the active site(s) through a manganous ion bridge.
Url:
DOI: 10.1016/0003-9861(69)90422-6
Affiliations:
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