Models for biological phosphoryl transfer

• Autorzy: Williams N H
• Języki publikacji: EN

Słowa kluczowe

EN

chemical biology; enzyme; phosphate; physiological condition; phosphoryl-transfer

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2003
• Tom: 08
• Numer: 2A
• Opis fizyczny: p.624-625

Twórcy

autor

Williams N H

• Sheffield University, Sheffield, S3 7HF, U.K.

Bibliografia

• 1. Lad, C., Williams, N.H. and Wolfenden, R.V. Rates of spontaneous hydrolysis of phosphate ester dianions and the extreme catalytic proficiencies of phosphatases involved in cell signaling and regulation. Proc. Natl. Acad. Sci. USA 100 (2003) 5607-5610.
• 2. Williams, N.H. and Wyman, P. Base catalysed phosphate diester hydrolysis. Chem. Comm. 14 (2001) 1268-1269.
• 3. Williams, N.H., Lebuis A-M. and Chin, J. A structural and functional model of dinuclear metallophosphatases. J. Am. Chem. Soc. 121 (1999) 3341-3348.
• 4. Humphry, T., Forconi, M., Williams N.H. and Hengge A.C. An altered mechanism of hydrolysis for a metal-complexed phosphate diester. J. Am. Chem. Soc. 124 (2002) 14860-14861.
• 5. Williams, N.H. Magnesium (II) catalysed ATP hydrolysis of ATP. J. Am. Chem. Soc. 122 (2000) 12023-12024.
• 6. Forconi, M. and Williams, N.H. Mimicking metallophosphatases: Revealing a role for an OH group with no libido. Angewandte Chemie, Int. Ed. Engl. 41 (2002) 849-852.