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Can I read Tryptophan in the Active Site of Rhodanese on EtoBox?
Tryptophan in the Active Site of Rhodanese by Betty Davidson; John Westley is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Tryptophan in the Active Site of Rhodanese about?
The transfer of sulfur from thiosulfate to cyanide is catalyzed by rhodanesel (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1). This reaction has been found to proceed by a double displacement mechanism (4, 5). Enzyme + 2 SSO,= e enzyme-& + 2 SOa-(1) Enzyme-S:! + 2 CN-= enzyme + 2 SCN-(2) Crystalline rhodanese was identified as the sulfur-enzyme intermediate. Other nucleophilic molecules, such as reduced lipoate, may replace cyanide in the reaction (1, 2). The present work was undertaken to study the nature of the enzyme-sulfur bond in the substituted enzyme intermediate. Evidence will be presented indicating that a tryptophyl residue in the active site of the enzyme is important in binding substrate sulfur. In addition, a cationic group may be implicated in the formation of the enzyme-thiosulfate complex. EXPERIMENTAL PROCEDURE Purification and Crystallization of Rhodanese-S2-Crystalline beef liver rhodanese was prepared by a modification of the method previously described (6). The major change was the omission of the acetone precipitation and preceding dialysis. This modification results in a 2.5-fold increase in the yield of crystalline enzyme. The enzyme obtained with this
Who reads Tryptophan in the Active Site of Rhodanese?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Betty Davidson; John Westley
- Publisher
- Elsevier BV
- Published
- 1965
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)