The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Synthesis and hydrolysis of malyl-coenzyme A by Pseudomonas AM1: an apparent malate synthase activity.

The malate synthase activity detectable in crude extracts of Pseudomonas AM1 has been shown to be due to a coupling of a malyl-CoA hydrolase with malyl-CoA lyase and not due to a discrete malate synthase enzyme. The partial purification of this malyl-CoA hydrolase from Pseudomonas AM1 has shown that it is distinct from citrate synthase which also hydrolyses malyl-CoA. The malyl-CoA hydrolase has a low Km for malyl-CoA (7-0 muM). A mutant of Pseudomonas AM1, ICT51 (Taylor & Anthony, 1975), which is unable to grow on ethanol, malonate or 3-hydroxybutyrate, has been shown to have an altered malyl-CoA hydrolase with a Km for malyl-CoA 30 times higher than that of the enzyme present in the wild-type organism. Two classes of revertants to growth on these substrates have been isolated: (i) those with a malyl-CoA hydrolase of similar Km to the wild-type and (ii) those in which the malyl-CoA hydrolase activity remains the same as in the mutant ICT51. The nature of the mutation leading to the latter class of revertants is unknown.[1]


WikiGenes - Universities