Enzymatic reactions involving novel mechanisms of carbanion stabilization. Academic Article

abstract

• The reactions catalyzed by orotidine monophosphate decarboxylase, oxalate decarboxylase, organomercurial lyase and phosphopantothenoylcysteine decarboxylase involve putative high-energy carbanion intermediates that cannot be stabilized by delocalization. Mechanistic and structural studies on each of these enzymes are described that suggest different strategies for carbanion stabilization. Both orotidine monophosphate decarboxylase and organomercurial lyase are likely to avoid carbanion formation by protonating the fragmenting bond, oxalate decarboxylase stabilizes an acyl carbanion using an adjacent radical and phosphopantothenoylcysteine decarboxylase stabilizes its carbanion by delocalization into a transient thioaldehyde.

authors

• Begley, Tadhg

published proceedings

• Curr Opin Chem Biol

author list (cited authors)

• Begley, T. P., & Ealick, S. E.

citation count

• 46

complete list of authors

• Begley, Tadhg P||Ealick, Steven E

publication date

• January 2004

publisher

• Elsevier  Publisher

published in

• Current Opinion in Chemical Biology  Journal

keywords

• Aldehydes
• Binding Sites
• Carboxy-Lyases
• Catalysis
• Lyases
• Molecular Structure
• Orotidine-5'-phosphate Decarboxylase
• Sulfhydryl Compounds

Digital Object Identifier (DOI)

• 10.1016/j.cbpa.2004.08.004

start page

• 508

end page

• 515

volume

• 8

issue

• 5

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.cbpa.2004.08.004