Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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- Name help_outline (2R)-2-hydroxy-2-methylbutanenitrile Identifier CHEBI:60908 Charge 0 Formula C5H9NO InChIKeyhelp_outline VMEHOTODTPXCKT-RXMQYKEDSA-N SMILEShelp_outline CC[C@@](C)(O)C#N 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline butan-2-one Identifier CHEBI:28398 (Beilstein: 741880; CAS: 78-93-3) help_outline Charge 0 Formula C4H8O InChIKeyhelp_outline ZWEHNKRNPOVVGH-UHFFFAOYSA-N SMILEShelp_outline CCC(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hydrogen cyanide Identifier CHEBI:18407 (CAS: 74-90-8) help_outline Charge 0 Formula CHN InChIKeyhelp_outline LELOWRISYMNNSU-UHFFFAOYSA-N SMILEShelp_outline C#N 2D coordinates Mol file for the small molecule Search links Involved in 45 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:28170 | RHEA:28171 | RHEA:28172 | RHEA:28173 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum.
Xu L.L., Singh B.K., Conn E.E.
The hydroxynitrile lyase (EC 4.1.2.--) which catalyzes the dissociation of the cyanohydrins of acetone and 2-butanone has been isolated and purified from young seedlings of flax (Linum usitatissimum L.). The purification procedure involved precipitation with (NH4)2SO4, chromatofocusing, and chroma ... >> More
The hydroxynitrile lyase (EC 4.1.2.--) which catalyzes the dissociation of the cyanohydrins of acetone and 2-butanone has been isolated and purified from young seedlings of flax (Linum usitatissimum L.). The purification procedure involved precipitation with (NH4)2SO4, chromatofocusing, and chromatography on DEAE-cellulose, hydroxylapatite, Sephacryl 200, and Matrex Red A gel columns with a final recovery of 21%. Purification of 136-fold yielded an apparently homogeneous preparation that, in contrast to the lyases isolated from Prunus species, is not a flavoprotein. The subunit molecular weight of 42,000 was estimated by gel electrophoresis in the presence of sodium dodecyl sulfate. The native molecular weight of the enzyme was estimated by gel filtration (HPLC) to be 82,000. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 degrees C. << Less
Arch. Biochem. Biophys. 263:256-263(1988) [PubMed] [EuropePMC]
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Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases.
Trummler K., Wajant H.
Acetone cyanohydrin lyase from Linum usitatissimum is a hydroxynitrile lyase (HNL) which is involved in the catabolism of cyanogenic glycosides in young seedlings of flax. We have isolated a full-length cDNA clone encoding L. usitatissimum HNL (LuHNL) from a cDNA expression library by immunoscreen ... >> More
Acetone cyanohydrin lyase from Linum usitatissimum is a hydroxynitrile lyase (HNL) which is involved in the catabolism of cyanogenic glycosides in young seedlings of flax. We have isolated a full-length cDNA clone encoding L. usitatissimum HNL (LuHNL) from a cDNA expression library by immunoscreening. LuHNL cDNA was expressed in Escherichia coli and isolated from the respective soluble fraction in an active form which was biochemically indistinguishable from the natural enzyme. An open reading frame of 1266 base pairs encodes for a protein of 45,780 kDa. The derived amino acid sequence shows no overall homologies to the to date cloned HNLs, but has significant similarities to members of the alcohol dehydrogenase (ADH) family of enzymes. In particular, the cysteine and histidine residues responsible for coordination of an active site Zn2+ and a second structurally important Zn2+ in alcohol dehydrogenases are conserved. Nevertheless, we found neither alcohol dehydrogenase activity in LuHNL nor HNL activity in ADH. Moreover, well known inhibitors of ADHs, which interfere with the coordination of the active site Zn2+, fail to affect HNL activity of LuHNL, suggesting principally different mechanisms of cyanohydrin cleavage and alcohol oxidation. Interestingly, LuHNL like ADH and Prunus serotina (PsHNL) possesses an ADP-binding betaalphabeta unit motif, pointing to the possibility that the non-flavoprotein PsHNL and the flavoprotein LuHNL have developed from two independent lines of evolution of a common ancestor with an ADP-binding betaalphabeta unit. << Less