H2N2V1, Istex, Corpus, bibRecord, 000E93

Inhibition of d-xylose isomerase by pentitols and d-lyxose

Identifieur interne : 000E93 ( Istex/Corpus ); précédent : 000E92; suivant : 000E94

Inhibition of d-xylose isomerase by pentitols and d-lyxose

Auteurs : Kei Yamanaka

Source :

Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1969.

RBID : ISTEX:2E9840EF56F39D36CCD0C0B09C9A9095DFBBB26A

English descriptors

Teeft :
- Biol, Brevis, Chem, Compulsory order, Inhibition studies, Inhibitor, Isomerase, Isomerase activity, Kyoto university, Michaelis, Pentitol, Pentitols, Previous paper, Ribitol, Xylitol, Yamanaka.

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:

https://api.istex.fr/ark:/67375/6H6-KQXSZHKV-8/fulltext.pdf

DOI: 10.1016/0003-9861(69)90422-6

Links to Exploration step

ISTEX:2E9840EF56F39D36CCD0C0B09C9A9095DFBBB26A

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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Inhibition of d-xylose isomerase by pentitols and d-lyxose

Inhibition of d-xylose isomerase by pentitols and d-lyxose

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