<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eb8 ConSurf].
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Revision as of 16:40, 8 February 2016
STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA
1eb8 is a 2 chain structure with sequence from Cassava. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Lauble H, Miehlich B, Forster S, Kobler C, Wajant H, Effenberger F. Structure determinants of substrate specificity of hydroxynitrile lyase from Manihot esculenta. Protein Sci. 2002 Jan;11(1):65-71. PMID:11742123
