1JU2

Crystal structure of the hydroxynitrile lyase from almond

Summary for 1JU2

• Entry DOI: 10.2210/pdb1ju2/pdb
• Descriptor: hydroxynitrile lyase, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• Functional Keywords: hydroxynitrile lyase, flavin, gmc oxidoreductase, almond, cyanogenesis, lyase
• Biological source: Prunus dulcis (almond)
• Total number of polymer chains: 2
• Total formula weight: 122581.05

Authors

Dreveny, I.,Gruber, K.,Glieder, A.,Thompson, A.,Kratky, C. (deposition date: 2001-08-23, release date: 2002-09-04, Last modification date: 2024-10-23)

Primary citation

Dreveny, I.,Gruber, K.,Glieder, A.,Thompson, A.,Kratky, C.
The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase.
Structure, 9:803-815, 2001

PubMed Abstract: 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.

PubMed: 11566130
DOI: 10.1016/S0969-2126(01)00639-6

Experimental method

X-RAY DIFFRACTION (1.47 Å)