English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A novel substrate, 6-(4-nitrophenyl)dihydropyrimidine-2,4(1 H ,3 H )-dione ( p NO 2 PheDU), was chemically synthesized and analytically verified for the potential biocatalytic synthesis of enantiopure  β -amino acids. The hydantoinase (EC 3.5.2.2) from  Arthrobacter crystallopoietes  DSM20117 was chosen to prove the enzymatic hydrolysis of this substrate, since previous investigations showed activities of this enzyme toward 6-monosubstituted dihydrouracils. Whole cell biotransformations with recombinant  Escherichia coli  expressing the hydantoinase showed degradation of  p NO 2 PheDU. Additionally, the corresponding  N -carbamoyl- β -amino acid ( N Carb p NO 2  β Phe) was chemically synthesized, an HPLC-method with chiral stationary phases for detection of this product was established and thus  (S) -enantioselectivity toward  p NO 2 PheDU has been shown. Consequently this novel substrate is a potential precursor for the enantiopure  β -amino acid  para -nitro- β -phenylalanine ( p NO 2  β Phe).   Electronic supplementary material  The online version of this article (doi:10.1186/s13568-015-0174-8) contains supplementary material, which is available to authorized users.

Chemical synthesis and enzymatic, stereoselective hydrolysis of a functionalized dihydropyrimidine for the synthesis of β-amino acids