Formaldehyde Dehydrogenase from Pseudomonas putida: The Role of A Cysteinyl Residue in the Enzyme Activity(Biological Chemistry)
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概要
- 論文の詳細を見る
Formaldehyde dehydrogenase from Pseudomonas putida C-83 was found to contain 7 halfcystine residues per subunit monomer, as checked by the method of performic acid oxidation. Approximately 7 sulfhydryl groups per subunit monomer were titrated with 5,5'-dithiobis(2-nitro benzoic acid) (DTNB) after denaturation with 8 M urea. In the native enzyme, modification of three sulfhydryl groups per subunit with ρ-chloromercuribenzoate (PCMB) led to the complete loss of enzyme activities for both formaldehyde and n-butanol. Hydrogen-peroxide competitively inhibited the enzyme activity for formaldehyde, while it was only slightly inhibitory to the activity for n-butanol. Both formaldehyde and hydrogen-peroxide protected one sulfhydryl group per subunit monomer from modification with PCMB. Moreover, hydrogen-peroxide was hardly reactive to the enzyme which was preincubated with formaldehyde. From these observations, we conclude that one of three PCMB-reactive sulfhydryl groups is essential for the binding of formaldehyde, and hydrogen-peroxide modifies this sulfhydryl group.
- 社団法人日本農芸化学会の論文
- 1986-10-23
著者
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ANDO Makoto
Research Division, Toyo Boseki Co., Ltd.
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Ogushi Susumu
Faculty Of Pharmaceutical Sciences Nagasaki University
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Tsuru D
School Of Pharmaceutical Sciences Nagasaki University:yakult Central Institute For Microbiological R
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Tsuru Daisuke
Faculty Of Pharmaceutical Sciences Nagasaki University
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Ando M
Department Of Applied Biological Chemistry Faculty Of Agriculture Shizuoka University
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Ando Makoto
Research Division Toyo Boseki Co. Ltd.
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