From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ju2.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ju2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ju2| PDB=1ju2 | SCENE= }} | | {{STRUCTURE_1ju2| PDB=1ju2 | SCENE= }} |
| | | | |
| - | '''Crystal structure of the hydroxynitrile lyase from almond'''
| + | ===Crystal structure of the hydroxynitrile lyase from almond=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | BACKGROUND: Cyanogenesis is a defense process of several thousand plant species. Hydroxynitrile lyase, a key enzyme of this process, cleaves a cyanohydrin into hydrocyanic acid and the corresponding aldehyde or ketone. The reverse reaction constitutes an important tool in biocatalysis. Different classes of hydroxynitrile lyases have convergently evolved from FAD-dependent oxidoreductases, alpha/beta hydrolases, and alcohol dehydrogenases. The FAD-dependent hydroxynitrile lyases (FAD-HNLs) carry a flavin cofactor whose redox properties appear to be unimportant for catalysis. RESULTS: We have determined the crystal structure of a 61 kDa hydroxynitrile lyase isoenzyme from Prunus amygdalus (PaHNL1) to 1.5 A resolution. Clear electron density originating from four glycosylation sites could be observed. As concerns the overall protein fold including the FAD cofactor, PaHNL1 belongs to the family of GMC oxidoreductases. The active site for the HNL reaction is probably at a very similar position as the active sites in homologous oxidases. CONCLUSIONS: There is strong evidence from the structure and the reaction product that FAD-dependent hydroxynitrile lyases have evolved from an aryl alcohol oxidizing precursor. Since key residues implicated in oxidoreductase activity are also present in PaHNL1, it is not obvious why this enzyme shows no oxidase activity. Similarly, features proposed to be relevant for hydroxy-nitrile lyase activity in other hydroxynitrile lyases, i.e., a general base and a positive charge to stabilize the cyanide, are not obviously present in the putative active site of PaHNL1. Therefore, the reason for its HNL activity is far from being well understood at this point.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11566130}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11566130 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11566130}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Gmc oxidoreductase]] | | [[Category: Gmc oxidoreductase]] |
| | [[Category: Hydroxynitrile lyase]] | | [[Category: Hydroxynitrile lyase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:55:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:51:51 2008'' |
Revision as of 17:51, 1 July 2008
Template:STRUCTURE 1ju2
Crystal structure of the hydroxynitrile lyase from almond
Template:ABSTRACT PUBMED 11566130
About this Structure
1JU2 is a Single protein structure of sequence from Prunus dulcis. Full crystallographic information is available from OCA.
Reference
The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase., Dreveny I, Gruber K, Glieder A, Thompson A, Kratky C, Structure. 2001 Sep;9(9):803-15. PMID:11566130
Page seeded by OCA on Tue Jul 1 20:51:51 2008
