myo-Inositol-1-phosphate synthase from pine pollen: sulfhydryl involvement at the active site
| Autor: | Mary W. Loewus, Subhash C. Gumber, Frank A. Loewus |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Binding Sites
biology ATP synthase Myo-Inositol-1-Phosphate Synthase Chemical Phenomena Chemistry Sulfhydryl Reagents Biophysics Active site Substrate (chemistry) Pine pollen Lyase Biochemistry Trees biology.protein Pollen NAD+ kinase Sulfhydryl Compounds Binding site Carbohydrate Epimerases Molecular Biology |
| Zdroj: | Archives of biochemistry and biophysics. 231(2) |
| ISSN: | 0003-9861 |
| Popis: | myo-Inositol-1-phosphate synthase [EC 5.5.1.4; 1L-myo-inositol-1-phosphate lyase, (isomerizing)] from Pinus ponderosa pollen has been partially purified and characterized. It has a pH optimum between 7.25 and 7.75. The km for d -glucose 6-phosphate (NAD+ constant at 1 m m ) is 0.33 m m . Inhibition by p-chloromercuribenzoate and N-ethyl-maleimide, and partial protection against this inhibition by d -glucose 6-phosphate in the presence of NAD+, suggests that there is sulfhydryl group involvement at the substrate binding site. |
| Databáze: | OpenAIRE |
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