Chemically reactive sulfhydryl groups of 1-aminocyclopropane-1-carboxylate deaminase.
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- HONMA Mamoru
- Department o] Agri cultural Chemistry, Hokkaido University
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説明
1-Aminocyclopropane-1-carboxylate deaminase was inhibited by several sulfhydryl-modifying reagents. Inhibition by 5, 5'-dithiobis(2-nitrobenzoic acid) were reversible. The chemically sensitive sulfhydryl groups were about 3 mol per mol of enzyme. A competitive inhibitor, L-serine, reduced modification of the sensitive sulfhydryl groups. The mechanism-based inhibition by β-chloro-Dalanine almost completely prevented the modification of sulfhydryl groups. The inhibition by monoiodoacetamide and N-ethylmaleimide was strengthened at pH values above 8.5, and in this range of pH, the maximum velocity of the enzyme reaction increased. <br> The enzyme had 2.8 mol of tightly bound pyridoxal 5'-phosphate per mol (110, 000 g) and was dissociated to a single subunit of molecular weight 36, 500 by sodium dodecyl sulfate. The purified enzyme showed pH-dependent absorption maxima at 326 and 416 run. The absorbance at 416 nm decreased as the pH of the enzyme solution increased from 7 to 9. The decrease in the absorbance corresponded to the pH dependence of Km and Ki at pH values below 8.5. The maximal affinity of the enzyme to substrate and competitive inhibitors, L-alanine and L-serine, was at pH 8.5.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 49 (3), 567-571, 1985
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206465784448
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- NII論文ID
- 130000026402
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- COI
- 1:CAS:528:DyaL2MXhvVWms74%3D
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- ISSN
- 18811280
- 00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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