Asymmetric synthesis of L-6-hydroxynorleucine from 2-keto-6-hydroxyhexanoic acid using a branched-chain aminotransferase

Title
Asymmetric synthesis of L-6-hydroxynorleucine from 2-keto-6-hydroxyhexanoic acid using a branched-chain aminotransferase
Author(s)
윤형돈서영만[서영만]김아란[김아란]배한섭[배한섭]이상협[이상협]
Keywords
EPSILON-HYDROXYNORLEUCINE; ENZYMATIC-SYNTHESIS; AMINO-ACIDS; TRANSAMINASES
Issue Date
201203
Publisher
INFORMA HEALTHCARE
Citation
BIOCATALYSIS AND BIOTRANSFORMATION, v.30, no.2, pp.171 - 176
Abstract
L-6-Hydroxynorleucine was synthesized from 2-keto-6-hydroxyhexanoic acid using branched-chain aminotransferase from Escherichia coli with L-glutamate as an amino donor. Since the branched-chain aminotransferase was severely inhibited by 2-ketoglutarate, the branched-chain aminotransferase reaction was coupled with aspartate aminotransferase and pyruvate decarboxylase. Aspartate aminotransferase converted the inhibitory 2-ketoglutarate back to L-glutamate by using L-aspartate as an amino donor. On the other hand, pyruvate decarboxylase further shifted the reaction equilibrium towards L-6-hydroxynorleucine through decarboxylation of pyruvate to acetaldehyde. The concerted action of the three enzymes significantly enhanced the yield compared to that of branched-chain aminotransferase alone. In the coupled reaction, 90.2 mM L-6-hydroxynorleucine (> 99% ee) was produced from 100 mM 2-keto-6-hydroxyhexanoic acid, whereas in a single branched-chain aminotransferase reaction only 22.5 mM L-6-hydroxynorleucine (> 99% ee) was produced.
URI
http://hdl.handle.net/YU.REPOSITORY/29597http://dx.doi.org/10.3109/10242422.2011.638373
ISSN
1024-2422
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생명공학부 > 생명공학부 > Articles
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