Chemical Communications 2006-04-28

A lag-phase in the reduction of flavin dependent thymidylate synthase (FDTS) revealed a mechanistic missing link.

Aaron Mason, Nitish Agrawal, M Todd Washington, Scott A Lesley, Amnon Kohen

Index: Chem. Commun. (Camb.) (16) , 1781-3, (2006)

Full Text: HTML

Abstract

An unexpected substrate-dependent lag-phase, found in the single turnover reduction of FDTS bound flavin, sheds light on the molecular mechanism of this alternative thymidylate synthase.

Related Compounds

Related Articles:

Simultaneous quantification of 5-FU, 5-FUrd, 5-FdUrd, 5-FdUMP, dUMP and TMP in cultured cell models by LC-MS/MS

2009-01-01

[J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 877 , 2937-2944, (2009)]

Ultrafast real-time visualization of active site flexibility of flavoenzyme thymidylate synthase ThyX.

2013-05-28

[Proc. Natl. Acad. Sci. U. S. A. 110(22) , 8924-9, (2013)]

Folate deficiency induces neurodegeneration and brain dysfunction in mice lacking uracil DNA glycosylase.

2008-07-09

[J. Neurosci. 28 , 7219-7230, (2008)]

Crystal structure and enzymatic characterization of thymidylate synthase X from Helicobacter pylori strain SS1.

2011-08-01

[Protein Sci. 20(8) , 1398-410, (2011)]

QM/MM study of thymidylate synthase: enzymatic motions and the temperature dependence of the rate limiting step.

2009-03-12

[J. Phys. Chem. A 113(10) , 2176-82, (2009)]

More Articles...