Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis
Material type:
TextPublication details: Proteins 1997Description: 438-449Subject(s): Online resources: Summary: (S)-Hydroxynitrile lyase (Hnl) from the rubber tree Hevea brasiliensis is a 29 kDa single chain protein that catalyses the breakdown or formation of a C(SINGLE BOND)C bond by reversible addition of hydrocyanic acid to aldehydes or ketones. The primary sequence of Hnl has no significant homology to known proteins. Detailed homology investigations employing PROFILESEARCH and secondary structure prediction algorithms suggest that Hnl is a member of the hydrolase fold protein family and contains a catalytic triad as functional residues was tested and confirmed by site-directed mutagenesis and expression of mutant and wildtype proteins in the yeast: Saccaromyces cerevisiae. Based on these data we suggest a mechanistic model for the (S)-cyanohydrin synthesis catalyzed by hydroxynitrile lyase from Hevea brasiliensis.
| Item type | Current library | Vol info | Status | |
|---|---|---|---|---|
Journals
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RRII Library Physiology | Volume 27, Issue 3 | Journals |
Source Year: 1998
(S)-Hydroxynitrile lyase (Hnl) from the rubber tree Hevea brasiliensis is a 29 kDa single chain protein that catalyses the breakdown or formation of a C(SINGLE BOND)C bond by reversible addition of hydrocyanic acid to aldehydes or ketones. The primary sequence of Hnl has no significant homology to known proteins. Detailed homology investigations employing PROFILESEARCH and secondary structure prediction algorithms suggest that Hnl is a member of the hydrolase fold protein family and contains a catalytic triad as functional residues was tested and confirmed by site-directed mutagenesis and expression of mutant and wildtype proteins in the yeast: Saccaromyces cerevisiae. Based on these data we suggest a mechanistic model for the (S)-cyanohydrin synthesis catalyzed by hydroxynitrile lyase from Hevea brasiliensis.
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