2009
DOI: 10.1016/j.molcatb.2009.01.007
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A highly enantioselective aminopeptidase from sunflower seed—Kinetic studies, substrate mapping and application to biocatalytic transformations

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Cited by 2 publications
(1 citation statement)
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“…In 2009 Tishinov and coworkers applied the major aminopeptidase from sunflower seed (Helianthus annuus L.) for the kinetic resolution of different a-amino acid amides [212]. Both racemic Phe-NH 2 and Phg-NH 2 were completely resolved by this enzyme into the (S)-acid and (R)-amide due to the absolute stereoselectivity of this enzyme for these two amides (E > 300).…”
Section: Synthesis Of Enantiopure A-h-a-amino Acidsmentioning
confidence: 99%
“…In 2009 Tishinov and coworkers applied the major aminopeptidase from sunflower seed (Helianthus annuus L.) for the kinetic resolution of different a-amino acid amides [212]. Both racemic Phe-NH 2 and Phg-NH 2 were completely resolved by this enzyme into the (S)-acid and (R)-amide due to the absolute stereoselectivity of this enzyme for these two amides (E > 300).…”
Section: Synthesis Of Enantiopure A-h-a-amino Acidsmentioning
confidence: 99%