Kinetic resolution of aromatic β-amino acids by ω-transaminase

Bea, Han-Seop; Park, Hye-Jeong; Lee, Sang‐Hyeup; Yun, Hyungdon

doi:10.1039/c1cc11528f

Cited by 61 publications

(44 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S2 in the supplemental material). These data show that VpAT is more active toward (S)-␤-phenylalanine than other ␤-transaminases reported previously (21,27,68). The activity of VpAT with pyruvate is 85% of that with ␣-ketoglutarate as the amino acceptor.…”

Section: Resultssupporting

confidence: 49%

“…These data suggest that VpAT, just like MesAT and PoGSAM, is a fold type I aminotransferase, and furthermore, that VpAT belongs to subgroup II transaminases, which is based on an enzyme's substrate specificity (27,48,68). VpAT has 19% sequence identity to a transaminase from Alcaligenes denitrificans that has been reported to have activity toward aliphatic ␤-amino acids (AdbpAT) (AAP92672.1) (21).…”

Section: Resultsmentioning

confidence: 89%

“…In addition, a sequence alignment between VpAT and a glutamate-1-semialdehyde-2,1-aminomutase from Polaromonas sp. JS666 (PoGSAM), for which no structure is available but which has activity toward aromatic ␤-amino acids (68), also showed conservation of R41 and E75 (as R51 and E85, respectively) (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

“…Sequence analysis showed that the enzyme is a fold type I AT, just like several other subgroup II -ATs. VpAT shows the highest sequence identity with biochemically characterized ␤-phenylalanine ATs (27,68), including the Mesorhizobium aminotransferase (MesAT), described by Kim et al (27), the structure of which was recently solved (48). MesAT and VpAT have similar activities with ␣-ketoglutarate and pyruvate as amino acceptors (27) but differ from ␣-transaminases, which generally show a clear preference for either pyruvate, ␣-ketoglutarate, or oxaloacetate (75)(76)(77).…”

Section: Catalytic Properties and Enantioselectivity Of Variovorax Atmentioning

confidence: 99%

See 3 more Smart Citations

Biochemical Properties and Crystal Structure of a β-Phenylalanine Aminotransferase from Variovorax paradoxus

Crismaru

Wybenga

Szymański

et al. 2013

Appl Environ Microbiol

View full text Add to dashboard Cite

e By selective enrichment, we isolated a bacterium that can use ␤-phenylalanine as a sole nitrogen source. It was identified by 16S rRNA gene sequencing as a strain of Variovorax paradoxus. Enzyme assays revealed an aminotransferase activity. Partial genome sequencing and screening of a cosmid DNA library resulted in the identification of a 1,302-bp aminotransferase gene, which encodes a 46,416-Da protein. The gene was cloned and overexpressed in Escherichia coli. The recombinant enzyme was purified and showed a specific activity of 17.5 U mg ؊1 for (S)-␤-phenylalanine at 30°C and 33 U mg ؊1 at the optimum temperature of 55°C. The ␤-specific aminotransferase exhibits a broad substrate range, accepting ortho-, meta-, and para-substituted ␤-phenylalanine derivatives as amino donors and 2-oxoglutarate and pyruvate as amino acceptors. The enzyme is highly enantioselective toward (S)-␤-phenylalanine (enantioselectivity [E], >100) and derivatives thereof with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic ␤-amino acids to yield (R)-␤-amino acids with >95% enantiomeric excess (ee). The crystal structures of the holoenzyme and of the enzyme in complex with the inhibitor 2-aminooxyacetate revealed structural similarity to the ␤-phenylalanine aminotransferase from Mesorhizobium sp. strain LUK. The crystal structure was used to rationalize the stereo-and regioselectivity of V. paradoxus aminotransferase and to define a sequence motif with which new aromatic ␤-amino acid-converting aminotransferases may be identified.

show abstract

Section: Resultssupporting

confidence: 49%

Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Catalytic Properties and Enantioselectivity Of Variovorax Atmentioning

confidence: 99%

See 2 more Smart Citations

Biochemical Properties and Crystal Structure of a β-Phenylalanine Aminotransferase from Variovorax paradoxus

Crismaru

Wybenga

Szymański

et al. 2013

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…14 This contributes to the library of a drug development tool with degradation resistance. 15 In the past decade, reports and reviews have been published on this topic, highlighting the possible strategies toward asymmetric synthesis of different kinds of substituted oxopyrrolidines in the optically active form. 5,16 Asymmetric organocatalysed Mannich reactions emerged as a powerful strategy in the construction of these building blocks via the formation of quaternary α-amino acids.…”

Section: Introductionmentioning

confidence: 99%

Stereoselective synthesis towards unnatural proline based amino acids

Makhathini¹,

Das²,

Singh³

et al. 2016

Arkivoc

View full text Add to dashboard Cite

A catalytic diastereoselective Mannich reaction promoted by chiral bifunctional urea-type organocatalysts has been developed. Treatment of N-Boc-3-ketoproline with N-Boc-aldimines under mild conditions afforded the corresponding unnatural proline based amino acid derivatives with excellent diastereoselectivities (up to 99:1) and enantioselectivities (up to 97% ee). The relative configuration of the chiral reaction products was deduced by the comparsion of the experimentally observed ECD spectra to that obtained theorectically.

show abstract