Identification of the Reactive Sulfhydryl Group of 1-Aminocyclopropane-1-carboxylate Deaminase
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概要
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1-Aminocyclopropane-1-carboxylgte (ACC) deaminase, a pyridoxal phosphate enzyme that catalyzes cyclopropane ring-opening and deamination of ACC, formed a quinoid intermediate with D-alanine, as shown by the appearance of a 510-nm absorption band. The presence of D-alanine also stimulated the inactivation of ACC deaminase with iodoacetamide. The increase of absorbance at 510 nm and the stimulation of the enzyme inactivation were temperature-dependent with a critical point at around 20℃, indicating a conformational change of the enzyme. To identify a reactive thiol group, this stimulated inactivation and an iodoacetamide derivative, N-(iodoacetamidoethyl)-1-aminonaphthalene-5-sulfonic acid were used. The residue that was modified by the specific reagent was monitored by absorbance at 350 nm through the digestion by lysylendopeptidase and the fractionation of peptides, and it was located at Cys-162 near the midpoint of the whole peptide chain of the ACC deaminase.
- 社団法人日本農芸化学会の論文
- 1993-12-23
著者
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HONMA Mamoru
Faculty of Agriculture, Hokkaido University
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KAWAI Jun
Faculty of Agriculture, Hokkaido University
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Honma Mamoru
Faculty Of Agriculture Hokkaido University
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Kawai Jun
Faculty Of Agriculture Hokkaido University
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Yamada Masataka
Faculty of Agriculture, Hokkaido University
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Yamada Masataka
Faculty Of Agriculture Hokkaido University
関連論文
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- Cloning and Sequencing of a cDNA Encoding α-Glucosidase from Sugar Beet
- Substitutions of Alanine for Cysteine at a Reactive Thiol Site and for Lysine at a Pyridoxal Phosphate Binding Site of 1-Aminocyclopropane-1-carboxylate Deaminase
- Chemical Modification and Amino Acid Sequence of Active Site in Sugar Beet α-Glucosidase
- Identification of the Reactive Sulfhydryl Group of 1-Aminocyclopropane-1-carboxylate Deaminase
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