133056-71-0Relevant academic research and scientific papers
Structure and mechanism of an unusual malonate decarboxylase and related racemases
Okrasa, Krzysztof,Levy, Colin,Hauer, Bernhard,Baudendistel, Nina,Leys, David,Micklefield, Jason
, p. 6609 - 6613 (2008)
A study was conducted to investigate the structure and mechanism of the arymalonate decarboxylase (AMDase), or malonate decarboxylase and related racemases. The AMDase is an unusual malonate decarboxylase, as it does not require biotin, or any other co-factors for activity and does not involve formation of a malonyl thioester-enzyme intermediate. It was found that the sequence of the AMDase shows similarity to the Glu and Asp rasmases. The fact that the AMDase and related Asp/Glu racemases do not require Mg2+, or any other co-factor, which might stabilize the postulated enediolate intermediate, made them unique enzymes for conducting investigations. It was also found that the homochiral carboxylic acid products of the AMDase are potentially valuable chiral precursors for the synthesis of pharmaceuticals and other products.
Design and evolution of an enzyme with a non-canonical organocatalytic mechanism
Burke, Ashleigh J.,Lovelock, Sarah L.,Frese, Amina,Crawshaw, Rebecca,Ortmayer, Mary,Dunstan, Mark,Levy, Colin,Green, Anthony P.
, p. 219 - 223 (2019/10/21)
The combination of computational design and laboratory evolution is a powerful and potentially versatile strategy for the development of enzymes with new functions1–4. However, the limited functionality presented by the genetic code restricts t
