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1dwo

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{{STRUCTURE_1dwo| PDB=1dwo | SCENE= }}
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'''CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS'''
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===CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11173464 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11173464}}
==About this Structure==
==About this Structure==
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[[Category: Acetone complex]]
[[Category: Acetone complex]]
[[Category: Hydroxynitrile lyase]]
[[Category: Hydroxynitrile lyase]]
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Revision as of 20:43, 30 June 2008

Image:1dwo.png

Template:STRUCTURE 1dwo

CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS

Template:ABSTRACT PUBMED 11173464

About this Structure

1DWO is a Single protein structure of sequence from Manihot esculenta. Full crystallographic information is available from OCA.

Reference

Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis., Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):194-200. PMID:11173464

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