Essential sulfhydryl groups in the active site of castor bean (Ricinus communis) seed acid phosphatase
作者： Paulo Afonso Granjeiro , Carmen Verı́ssima Ferreira , Alexandre Donizeti Martins Cavagis , José Mauro Granjeiro , Hiroshi Aoyama
DOI: 10.1016/S0168-9452(03)00016-5
关键词: Biology 、 Enzyme assay 、 Biochemistry 、 Active site 、 Iodoacetic acid 、 Phenylglyoxal 、 Amino acid 、 Tryptophan 、 Acid phosphatase 、 Enzyme catalysis
摘要: Abstract In order to determine which amino acids are involved in substrate binding, castor bean seeds acid phosphatase was treated with acid-modifying reagents, such as phenylglyoxal (PGO), iodoacetic (IAA), N-bromosuccinimide (NBS), N-acetylimidazole (NAI), diethylpyrocarbonate (DEPC), N,N′-dicyclohexylcarbodiimide (DCCD) and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC), specific for arginine, cysteine, tryptophan, tyrosine, histidine, aspartic glutamic acids, respectively. Enzyme activity determined using p -nitrophenylphosphate ( NPP) substrate. inhibition observed IAA, NBS, EDC DCCD. the presence of reaction products, -nitrophenol NP) inorganic phosphate (Pi), competitive inhibitors, enzyme protected from inactivation by indicating involvement active site. The IAA time- concentration-dependent, an apparent bimolecular rate constant 48×10 −4 M −1 s , two molecules bound per Our results suggest that sulfhydryl groups essential catalysis, located or near substrate-binding domain. Other were also important activity, but probably outside
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