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Racemase Activity o...
Racemase Activity of B. cepacia Lipase Leads to Dual-Function Asymmetric Dynamic Kinetic Resolution of alpha-Aminonitriles
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- Vongvilai, Pornrapee (author)
- KTH,Organisk kemi
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- Linder, Mats (author)
- KTH,Fysikalisk kemi
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- Sakulsombat, Morakot (author)
- KTH,Organisk kemi
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- Humble, Maria Svedendahl (author)
- KTH,Biokemi
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- Berglund, Per (author)
- KTH,Biokemi
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- Brinck, Tore (author)
- KTH,Fysikalisk kemi
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- Ramström, Olof (author)
- KTH,Organisk kemi
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(creator_code:org_t)
- 2011-06-01
- 2011
- English.
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In: Angewandte Chemie International Edition. - : Wiley. - 1433-7851 .- 1521-3773. ; 50:29, s. 6592-6595
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
Close
- Applaudable promiscuity: Racemase-type activity discovered for B. cepacia lipase with N-substituted α-aminonitriles is proposed to involve a C-C bond-breaking/forming mechanism in the hydrolase site of the enzyme, as supported by experimental data and calculations. This promiscuous activity in combination with the transacylation activity of the enzyme enabled the asymmetric synthesis of N-methyl α-aminonitrile amides in high yield (see scheme).
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Keyword
- dynamic kinetic resolution
- enzyme catalysis
- racemase activity
- secondary amines
- Strecker reaction
- Chemistry
- Kemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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