The interaction of monofluorofumarate with adenylosuccinate lyase. Academic Article

abstract

• Monofluorofumarate was tested as an alternate substrate and inhibitor for adenylosuccinate lyase. Monofluorofumarate was found to be a slow reacting substrate when either AMP or AICAR (5-aminoimidazole 4-carboxamide ribonucleotide) were used as substrate acceptor molecules at pH 7.5. There was no indication that monofluorofumarate could induce the inactivation of adenylosuccinate lyase. The initial reaction product when monofluorofumarate was incubated with AMP in the presence of adenylosuccinate lyase has been determined to be 2-fluoro-adenylosuccinate. This molecule lost HF spontaneously, and the subsequent intermediate was rapidly hydrolyzed to oxalacetate and AMP. A similar reaction scheme was also observed when AICAR was utilized as a cosubstrate with monofluorofumarate. The initial reaction rate when 1.0 mM monofluorofumarate and 1.0 mM AMP were used as substrates with adenylosuccinate lyase was only 1.4% of the rate when 1.0 mM fumarate was used. AICAR (1.0 mM) was found to react with monofluorofumarate at 8.9% of the rate that it reacts with fumarate.

authors

• Raushel, Frank

published proceedings

• J Enzyme Inhib

author list (cited authors)

• Kim, S. C., & Raushel, F. M.

citation count

• 2

complete list of authors

• Kim, SC||Raushel, FM

publication date

• January 1988

publisher

• Taylor & Francis  Publisher

published in

• J Enzyme Inhib  Journal

keywords

• Adenosine Monophosphate
• Adenylosuccinate Lyase
• Fumarates
• Kinetics
• Lyases
• Spectrophotometry, Ultraviolet

Digital Object Identifier (DOI)

• 10.3109/14756368809040721

start page

• 153

end page

• 161

volume

• 2

issue

• 3

URL

• http://dx.doi.org/10.3109/14756368809040721