Article
Kinetic, mutational, and structural analysis of malonate semialdehyde decarboxylase from Coryneform bacterium strain FG41: mechanistic implications for the decarboxylase and hydratase activities.
Biochemistry - 16 Jul 2013
Guo Youzhong, Serrano Hector, Poelarends Gerrit J, Johnson William H, Hackert Marvin L, Whitman Christian P
Abstract excerpt
Malonate semialdehyde decarboxylase from Pseudomonas pavonaceae 170 (designated Pp MSAD) is in a bacterial catabolic pathway for the nematicide 1,3-dichloropropene. MSAD has two known activities: it catalyzes the metal ion-independent decarboxylation of malonate semialdehyde to produce acetaldehyde and carbon dioxide and a low-level hydration of 2-oxo-3-pentynoate to yield acetopyruvate. The latter activity is...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.