1eb8
From Proteopedia
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| - | [[Image:1eb8.jpg|left|200px]] | + | [[Image:1eb8.jpg|left|200px]] |
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| - | '''STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA''' | + | {{Structure |
| + | |PDB= 1eb8 |SIZE=350|CAPTION= <scene name='initialview01'>1eb8</scene>, resolution 2.10Å | ||
| + | |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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE DETERMINANTS OF SUBSTRATE SPECIFICITY OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EB8 is a [ | + | 1EB8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Manihot_esculenta Manihot esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EB8 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11742123 11742123] |
[[Category: Manihot esculenta]] | [[Category: Manihot esculenta]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:59 2008'' |
Revision as of 08:53, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Transferred entry: 3.3.2.4, with EC number 4.2.1.37 | ||||||
| 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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