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2. Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomerase. Poddar H; Rahimi M; Geertsema EM; Thunnissen AM; Poelarends GJ Chembiochem; 2015 Mar; 16(5):738-41. PubMed ID: 25728471 [TBL] [Abstract][Full Text] [Related]
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8. Inter- and intramolecular aldol reactions promiscuously catalyzed by a proline-based tautomerase. Rahimi M; Geertsema EM; Miao Y; van der Meer JY; van den Bosch T; de Haan P; Zandvoort E; Poelarends GJ Org Biomol Chem; 2017 Mar; 15(13):2809-2816. PubMed ID: 28277572 [TBL] [Abstract][Full Text] [Related]
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14. Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase. Poelarends GJ; Almrud JJ; Serrano H; Darty JE; Johnson WH; Hackert ML; Whitman CP Biochemistry; 2006 Jun; 45(25):7700-8. PubMed ID: 16784221 [TBL] [Abstract][Full Text] [Related]
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17. Mutants of 4-oxalocrotonate tautomerase catalyze the decarboxylation of oxaloacetate through an imine mechanism. Brik A; D'Souza LJ; Keinan E; Grynszpan F; Dawson PE Chembiochem; 2002 Sep; 3(9):845-51. PubMed ID: 12210985 [TBL] [Abstract][Full Text] [Related]
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20. Mutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations. Rahimi M; van der Meer JY; Geertsema EM; Poddar H; Baas BJ; Poelarends GJ Chembiochem; 2016 Jul; 17(13):1225-8. PubMed ID: 27238293 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]