Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2- …

…, F Kroll, G Bröker, B Beatrix, W Buckel, BT Golding

Index: Ciceri, Daniele; Pierik, Antonio J.; Hartrampf, Guenter; Broeker, Gerd; Speranza, Giovanna; Buckel, Wolfgang; Cornforth, Sir John; Golding, Bernard T. Helvetica Chimica Acta, 2000 , vol. 83, # 9 p. 2550 - 2561

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Citation Number: 17

Abstract

Coenzyme B12-dependent 2-methyleneglutarate mutase from the strict anaerobe Eubacterium barkeri catalyzes the equilibration of 2-methyleneglutarate with (R)-3- methylitaconate. Proteins with mutations in the highly conserved coenzyme binding-motif DXH (X) 2G (X) 41GG (D483N and H485Q) exhibited decreased substrate turnover by 2000- fold and> 4000-fold, respectively. These findings are consistent with the notion of H485 ...