1dwq

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==Overview==
==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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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.
==About this Structure==
==About this Structure==
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[[Category: Manihot esculenta]]
[[Category: Manihot esculenta]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Transferred entry: 3.3.2.4]]
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[[Category: Transferred entry: 3 3.2 4]]
[[Category: Effenberger, F.]]
[[Category: Effenberger, F.]]
[[Category: Forster, S.]]
[[Category: Forster, S.]]
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[[Category: hydroxynitrile lyase]]
[[Category: hydroxynitrile lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:35:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:18 2008''

Revision as of 10:21, 21 February 2008


1dwq, resolution 2.2Å

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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

Overview

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.

About this Structure

1DWQ is a Single protein structure of sequence from Manihot esculenta with as ligand. Active as Transferred entry: 3.3.2.4, with EC number 4.2.1.37 Known structural/functional Sites: and . 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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