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0343788128
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[Title translation: On the kinetics of the synthesis of (+)-mandelonitrile accelerated by emulsin.]
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[Title translation: On the flavinenzyme D-oxynitrilase.]
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••] contain details of successful overexpression of the LuHnl and have assigned this enzyme to a novel class of Hnl, which is related to zinc-dependent alcohol dehydrogenases. This work has also allowed extensive substrate studies to be performed using aromatic and aliphatic aldehydes as well as ketones.
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••] contain details of successful overexpression of the LuHnl and have assigned this enzyme to a novel class of Hnl, which is related to zinc-dependent alcohol dehydrogenases. This work has also allowed extensive substrate studies to be performed using aromatic and aliphatic aldehydes as well as ketones.
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The expression of the LuHnl in Escherichia coli is described. Upon determination of the amino-acid sequence, the enzyme was found to be homologous to the zinc-dependent formaldehyde dehydrogenases. In addition, an enzyme with a relatively high specific activity (76 U/mg) was obtained.
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Breithaupt H., Pohl M., Bönigk W., Heim P., Schimz K-L., Kula M-R. Cloning and expression of (R)-hydroxynitrile lyase from Linium usitatissimum (flax). J Mol Catal B. 6:1999;315-332. The expression of the LuHnl in Escherichia coli is described. Upon determination of the amino-acid sequence, the enzyme was found to be homologous to the zinc-dependent formaldehyde dehydrogenases. In addition, an enzyme with a relatively high specific activity (76 U/mg) was obtained.
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This paper compares the performance of three Hnls (from almond, peach and loquat) with a number of aromatic or aliphatic and ketones as substrates in diisopropyl ether. In general, the new sources of (R)-Hnl (i.e. peach and loquat) perform favorably compared to the more established source (almonds).
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Lin G., Han S., Li Z. Enzymatic synthesis of (R)-cyanohydrins by three (R)-oxynitrilase sources in micro-aqueous organic medium. Tetrahedron. 55:1999;3531-3540. This paper compares the performance of three Hnls (from almond, peach and loquat) with a number of aromatic or aliphatic and ketones as substrates in diisopropyl ether. In general, the new sources of (R)-Hnl (i.e. peach and loquat) perform favorably compared to the more established source (almonds).
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•] investigate the challenging problem of enzymatic diastereomeric cyanohydrin formation in a systematic fashion for the first time.
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•] investigate the challenging problem of enzymatic diastereomeric cyanohydrin formation in a systematic fashion for the first time.
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24
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0033462190
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Almond oxynitrilase-catalyzed transformation of aldehydes is strongly influenced by naphtyl and alkoxy substituents
-
Different α-substituted and β-substituted aldehydes have been studied with the PaHnl. These studies explored the influence of a stereocenter already present in the substrate on the selectivity of this enzyme. The results indicate that such substitutions have a significant influence on the stereochemical outcome of the reaction.
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Roda G., Riva S., Danieli B. Almond oxynitrilase-catalyzed transformation of aldehydes is strongly influenced by naphtyl and alkoxy substituents. Tetrahedron - Asymmetry. 10:1999;3939-3949. Different α-substituted and β-substituted aldehydes have been studied with the PaHnl. These studies explored the influence of a stereocenter already present in the substrate on the selectivity of this enzyme. The results indicate that such substitutions have a significant influence on the stereochemical outcome of the reaction.
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Griengl H., Klempier N., Pöchlauer P., Schmidt M., Shi N., Zabelinskaja-Mackova A.A. Enzyme catalysed formation of (S)-cyanohydrins derived from aldehydes and ketones in a biphasic solvent system. Tetrahedron. 54:1998;14477-14486.
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Book of abstracts, July 23-28, Göteborg
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Mackova-Zabelinskaja A.A, Griengl H, Kern W: Asymmetric synthesis of cyanohydrins of ketones using (S)-hydroxynitrile lyase from Hevea brasiliensis. Book of abstracts, Poster 108, 11th European Symposium on Organic Chemistry, 1999 July 23-28, Göteborg.
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0032530859
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Hydroxynitrile lyase adsorption at liquid/liquid interfaces
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The authors describe novel techniques of measurement (i.e. interfacial tension measurements between a buffer and an organic phase) with the PaHnl in order to observe possible changes in its structure and to delineate where the enzymatic reaction occurs.
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Hickel A., Radke C.J., Blanch H.W. Hydroxynitrile lyase adsorption at liquid/liquid interfaces. J Mol Catal B. 5:1998;349-354. The authors describe novel techniques of measurement (i.e. interfacial tension measurements between a buffer and an organic phase) with the PaHnl in order to observe possible changes in its structure and to delineate where the enzymatic reaction occurs.
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Hickel A., Radke C.J., Blanch H.W. Hydroxynitrile lyase at the diisopropyl ether water interface: evidence for interfacial enzyme activity. Biotechnol Bioeng. 65:1999;425-435.
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Bauer M., Geyer R., Boy M., Griengl H., Steiner W. Stability of the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis. J Mol Catal B. 5:1998;343-347.
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Bauer M., Greingl H., Steiner W. Parameters influencing stability and activity of a (S)-hydroxynitrile lyase from Hevea brasiliensis in two-phase systems. Enzyme Microb Technol. 24:1999;514-522.
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Costes D., Wehtje E., Aldlercreutz P. Hydroxynitrile lyase-catalysed synthesis of cyanohydrins in organic solvents: parameters influencing activity and enantiospecificity. Enzyme Microb Technol. 25:1999;384-391.
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0032852375
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3D structure of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis
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This paper, along with [38], reveals new insight into the enzyme catalysed cyanohydrin formation reaction. The authors describe the crystal structures of enzyme-substrate complexes and outline an updated mechanistic proposal in which two amino-acid residues, Thr11 and His235, have an additional role to play.
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Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C. 3D structure of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis. Protein Sci. 8:1999;1990-2000. This paper, along with [38], reveals new insight into the enzyme catalysed cyanohydrin formation reaction. The authors describe the crystal structures of enzyme-substrate complexes and outline an updated mechanistic proposal in which two amino-acid residues, Thr11 and His235, have an additional role to play.
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Zuegg, J.1
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38
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0032847750
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Gruber K., Gugganig M., Wagner U.G., Kratky C. Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Biol Chem. 380:1999;993-1000.
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0345310065
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Chemoenzymatic synthesis of (S)-2-cyanopiperidine, a key intermediate in the route to (S)-pipecolic acid and 2-substituted piperidine alkaloids
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An efficient route to piperidine alkaloid intermediates employing both an intramolecular and intermolecular substitution is described in this article.
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Nazabadioko S., Perez R.J., Brieva R., Gotor V. Chemoenzymatic synthesis of (S)-2-cyanopiperidine, a key intermediate in the route to (S)-pipecolic acid and 2-substituted piperidine alkaloids. Tetrahedron - Asymmetry. 9:1999;1597-1604. An efficient route to piperidine alkaloid intermediates employing both an intramolecular and intermolecular substitution is described in this article.
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Nazabadioko, S.1
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40
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0001942469
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This paper describes the novel conversion of chiral cyanohydrins to α-hydroxynitrones, followed by a selective intramolecular cyclisation.
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Marcus J., Brussee J., van der Gen A. Intramolecular cycloaddition reactions of w-unsaturated chiral nitrones. Eur J Org Chem. 1:1998;2513-2517. This paper describes the novel conversion of chiral cyanohydrins to α-hydroxynitrones, followed by a selective intramolecular cyclisation.
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van der Nieuwendijk A.M.C.H., Benningshof J.C.J., Wegmann V., Bank R.A., te Koppele J.M., Brussee J., van der Gen A. Synthesis of reduced collagen crosslinks. Bioorg Med Chem Lett. 9:1999;1673-1676.
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Effenberger F., Gaupp S. Stereoselective substitution of (R)-2-(sulfonyloxy)nitriles with sulfur nucleophiles. Tetrahedron - Asymmetry. 10:1999;1765-1775.
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43
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Gaupp S., Effenberger F. Stereoselective follow-up reactions of (S)-2-sulfanyl nitriles. Tetrahedron - Asymmetry. 10:1999;1777-1786.
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Johnson D.V., Felfer U., Griengl H. A chemoenzymatic access to D- and L-sphingosines employing hydroxynitrile lyases. Tetrahedron. 56:2000;. in press.
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