| Title : Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis - Lauble_2001_Acta.Crystallogr.D.Biol.Crystallogr_57_194 |
| Author(s) : Lauble H , Forster S , Miehlich B , Wajant H , Effenberger F |
| Ref : Acta Crystallographica D Biol Crystallogr , 57 :194 , 2001 |
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Abstract :
The crystal structures of hydroxynitrile lyase from Manihot esculenta (MeHNL) complexed with the native substrate acetone and substrate analogue chloroacetone have been determined and refined at 2.2 A resolution. The substrates are positioned in the active site by hydrogen-bond interactions of the carbonyl O atom with Thr11 OG, Ser80 OG and, to a lesser extent, Cys81 SG. These studies support a mechanism for cyanogenesis as well as for the stereospecific MeHNL-catalyzed formation of (S)-cyanohydrins, which closely resembles the base-catalyzed chemical reaction of HCN with carbonyl compounds. |
| PubMedSearch : Lauble_2001_Acta.Crystallogr.D.Biol.Crystallogr_57_194 |
| PubMedID: 11173464 |
| Gene_locus related to this paper: manes-hnl |
Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F (2001)
Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis
Acta Crystallographica D Biol Crystallogr
57 :194
Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F (2001)
Acta Crystallographica D Biol Crystallogr
57 :194