1eb8

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|SITE= <scene name='pdbsite=ASA:Residues+Involved+In+Catalysis+Site+For+Chain+B'>ASA</scene>
|SITE= <scene name='pdbsite=ASA:Residues+Involved+In+Catalysis+Site+For+Chain+B'>ASA</scene>
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.3.2.4 Transferred entry: 3.3.2.4], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.37 4.2.1.37]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-epoxysuccinate_hydrolase Trans-epoxysuccinate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.4 3.3.2.4] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb8 OCA], [http://www.ebi.ac.uk/pdbsum/1eb8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eb8 RCSB]</span>
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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: Trans-epoxysuccinate hydrolase]]
[[Category: Effenberger, F.]]
[[Category: Effenberger, F.]]
[[Category: Foerster, S.]]
[[Category: Foerster, S.]]
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[[Category: Miehlich, B.]]
[[Category: Miehlich, B.]]
[[Category: Wajant, H.]]
[[Category: Wajant, H.]]
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[[Category: MPD]]
 
[[Category: active-site tunnel mutant]]
[[Category: active-site tunnel mutant]]
[[Category: hydroxynitrile lyase]]
[[Category: hydroxynitrile lyase]]
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[[Category: substrate specificity]]
[[Category: substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:07 2008''

Revision as of 16:59, 30 March 2008


PDB ID 1eb8

Drag the structure with the mouse to rotate
, resolution 2.10Å
Sites:
Ligands:
Activity: Trans-epoxysuccinate hydrolase, with EC number 3.3.2.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA


Overview

Tryptophan 128 of hydroxynitrile lyase of Manihot esculenta (MeHNL) covers a significant part of a hydrophobic channel that gives access to the active site of the enzyme. This residue was therefore substituted in the mutant MeHNL-W128A by alanine to study its importance for the substrate specificity of the enzyme. Wild-type MeHNL and MeHNL-W128A showed comparable activity on the natural substrate acetone cyanohydrin (53 and 40 U/mg, respectively). However, the specific activities of MeHNL-W128A for the unnatural substrates mandelonitrile and 4-hydroxymandelonitrile are increased 9-fold and approximately 450-fold, respectively, compared with the wild-type MeHNL. The crystal structure of the MeHNL-W128A substrate-free form at 2.1 A resolution indicates that the W128A substitution has significantly enlarged the active-site channel entrance, and thereby explains the observed changes in substrate specificity for bulky substrates. Surprisingly, the MeHNL-W128A--4-hydroxybenzaldehyde complex structure at 2.1 A resolution shows the presence of two hydroxybenzaldehyde molecules in a sandwich type arrangement in the active site with an additional hydrogen bridge to the reacting center.

About this Structure

1EB8 is a Single protein structure of sequence from Manihot esculenta. Full crystallographic information is available from OCA.

Reference

Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta., Lauble H, Miehlich B, Forster S, Kobler C, Wajant H, Effenberger F, Protein Sci. 2002 Jan;11(1):65-71. PMID:11742123

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