Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis (Record no. 60558)

MARC details
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fixed length control field 01368nam a2200205Ia 4500
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Personal name Hasslacher M
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Title Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Name of publisher Proteins
Year of publication 1997
300 ## - PHYSICAL DESCRIPTION
Number of Pages 438-449
500 ## - GENERAL NOTE
General note Source Year: 1998
520 ## - SUMMARY, ETC.
Summary, etc (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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Topical Term Hevea brasiliensis
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Personal name Griengl H
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Personal name Kohlwein S D
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Personal name Kratky C
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Personal name Schwab
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Uniform Resource Identifier IRRDB
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type Journals
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Holdings
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