CAS: 2481-10-9; H-Cys(Tbu)-Oh

上下游产品

S-t-butyl-L-cysteine t-butyl ester S-tert-Butyl-L-cysteine tert-Butyl Ester Hydr°Chloride L-Cysteine tert-butyl alcoholtert-butyl alcoholL-cystine N-(Carbo-tert-butoxy)-S-tert-butyl-L-cysteine 2-methylpropan-2-thiol 2-oxo-propionic acid

📜S-Tert-Butyl-N-Acetyl-L-Cysteine置于pig Kidney Acylase I体系中,用 Phosphate Buffer 用作溶剂,化学反应 0.17H,反应生成D-S-叔丁基半胱氨酸
参考文献:Acylase I-Catalyzed Deacetylation Of N-Acetyl-L-Cysteine And S-Alkyl-N-Acetyl-L-Cysteines
标题:Acylase I-Catalyzed Deacetylation Of N-Acetyl-L-Cysteine And S-Alkyl-N-Acetyl-L-Cysteines
摘要:The Aminoacylase That Catalyzes The Hydrolysis Of N-Acetyl-L-Cysteine (Nac) Was Identified As Acylase I After Purification By Column Chromatography And Electrophoretic Analysis. Rat Kidney Cytosol Was Fractionated By Ammonium Sulfate Precipitation,And The Proteins Were Separated By Ion-Exchange Column Chromatography,Gel-Filtration Column Chromatography,And Hydrophobic Interaction Column Chromatography. Acylase Activity With Nac And N-Acetyl-L-Methionine (Nam),A Known Substrate For Acylase I,As Substrates Coeluted During All Chromatographic Steps. Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis Showed That The Protein Was Purified To Near Homogeneity And Had A Subunit M-R Of 43 000,Which Is Identical With The M-R Of Acylase I From Porcine Kidney And Bovine Liver. N-Butylmalonic Acid Was A Slow-Binding Inhibitor Of Acylase I And Inhibited The Deacetylation Of Nac With A K-I Of 192 +/-27 Mu M These Results Show That Acylase I Catalyzes The Deacetylation Of Nag. The Acylase I-Catalyzed Deacetylation Of A Range Of S-Alkyl-N-Acetyl-L-Cysteines,Their Carbon And Oxygen Analogues,And The Selenium Analogue Of Nam Was Also Studied With Porcine Kidney Acylase I. The Specific Activity Of The Acylase I-Catalyzed Deacetylation Of These Substrates Was Related To Their Calculated Molar Volumes And Lag P Values. The S-Alkyl-N-Acetyl-L-Cysteines With Short (C-0-C-3) And Unbranched S-Alkyl Substituents Were Good Acylase I Substrates,Whereas The S-Alkyl-N-Acetyl-L-Cysteines With Long (>C-3) And Branched S-Alkyl Substituents Were Poor Acylase I Substrates. The Carbon And Oxygen Analogues Of S-Methyl-N-Acetyl-L-Cysteine And The Carbon Analogue Of S-Ethyl-N-Acetyl-L-Cysteine Were Poor Acylase I Substrates,Whereas The Selenium Analogue Of Nam Was A Good Acylase I Substrate.
Doi:10.1021/tx980018B