Stereoselective synthesis of l-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase

Hsu, Shih-Kuang; Lo, Hsueh-Hsia; Lin, Wei‐De; Chen, I-Chien; Kao, Chien-Han; Hsu, Wen-Hwei

doi:10.1016/j.procbio.2007.02.008

Cited by 19 publications

(9 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recombinant plasmids were then introduced into E. coli NovaBlue and induced by the addition of 0.5 mM IPTG and incubation at 30°C for 6 h. The recombinant proteins in the crude extract were purified by nickel chelate affinity chromatography. The activities of NAAAR and NAGPR were assayed by methods described previously (18,34). The results showed that purified Lyr 188-393 and NAGPR had about 50% of the specific activity of E. coli NAGPR, while the purified NAAAR , Lyr, and Lyr proteins displayed no racemization activity toward chiral (Table 2).…”

mentioning

confidence: 99%

Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library

Chen

Lin

Hsu

et al. 2009

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids with a molecular mass of about 42.7 kDa. The enzyme exhibited higher specific activity toward lysine in the L-lysine-to-D-lysine direction than in the reverse reaction.

show abstract

mentioning

confidence: 99%

Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library

Chen

Lin

Hsu

et al. 2009

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

show abstract

“…•h −1 (Figure 2B, Hsu et al, 2007). Engineered NSAR (G291D/F323Y mutant) from Amycolatopsis sp., together with D-acylase (Chirotech Technology Ltd) allowed conversion of N-acetyl-D,L-allylglycine (50 g•L −1 ) into D-allylglycine in 18 h with a 98% conversion ( Figure 2C, Baxter et al, 2012).…”

Section: Amidohydrolase Processmentioning

confidence: 99%

“…(B) L-homophenylalanine production by NSAR/L-acylase tandem. Whole cell biocatalyst containing N-succinyl-amino acid racemase (NSAR) and L-acylase (L-Acyl) from Deinococcus radiodurans were used, starting from racemic N-acetyl-L-homophenylalanine (Hsu et al, 2007). (C) D-allylglycine production by NSAR/D-acylase tandem, consisting of pure D-acylase (D-Acyl, Chirotech Technology Ltd.) and an engineered N-succinyl-amino acid racemase from Amycolatopsis sp (NSAR, G291D/F323Y mutant; Baxter et al, 2012).…”

Section: Amidase Processmentioning

confidence: 99%

“…An E. coli whole cell system comprising a NSAR/L-acylase from Deinococcus radiodurans was used to produce L -homophenylalanine with a 99.9% yield and over 99% e.e. (in 1 h), with a productivity of 10 mmol⋅L –1 ⋅h –1 ( Figure 2B , Hsu et al, 2007 ). Engineered NSAR (G291D/F323Y mutant) from Amycolatopsis sp., together with D -acylase (Chirotech Technology Ltd) allowed conversion of N -acetyl- D,L -allylglycine (50 g⋅L –1 ) into D -allylglycine in 18 h with a 98% conversion ( Figure 2C , Baxter et al, 2012 ).…”

Section: Multienzymatic Cascades For the Production Of Ncaasmentioning

confidence: 99%

See 1 more Smart Citation

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Martínez‐Rodríguez

Torres

Sánchez

et al. 2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

The 22 genetically encoded amino acids (AAs) present in proteins (the 20 standard AAs together with selenocysteine and pyrrolysine), are commonly referred as proteinogenic AAs in the literature due to their appearance in ribosome-synthetized polypeptides. Beyond the borders of this key set of compounds, the rest of AAs are generally named imprecisely as non-proteinogenic AAs, even when they can also appear in polypeptide chains as a result of post-transductional machinery. Besides their importance as metabolites in life, many of D-α-and L-α-"non-canonical" amino acids (NcAAs) are of interest in the biotechnological and biomedical fields. They have found numerous applications in the discovery of new medicines and antibiotics, drug synthesis, cosmetic, and nutritional compounds, or in the improvement of protein and peptide pharmaceuticals. In addition to the numerous studies dealing with the asymmetric synthesis of NcAAs, many different enzymatic pathways have been reported in the literature allowing for the biosynthesis of NcAAs. Due to the huge heterogeneity of this group of molecules, this review is devoted to provide an overview on different established multienzymatic cascades for the production of non-canonical D-α-and L-α-AAs, supplying neophyte and experienced professionals in this field with different illustrative examples in the literature. Whereas the discovery of new or newly designed enzymes is of great interest, dusting off previous enzymatic methodologies by a "back and to the future" strategy might accelerate the implementation of new or improved multienzymatic cascades.

show abstract

“…Based on this fact, a D. radiodurans N-acylamino acid racemase with racemization activity toward chiral N-carbamoyl-homophenylalanine [33] was also introduced into the process for the improvement of L-HPA production. As shown in Fig.…”

Section: Conversion Of Dl-hpah To L-hpamentioning

confidence: 99%

Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine

Kao

Wang

et al. 2009

Process Biochemistry

Self Cite

View full text Add to dashboard Cite

Stereoselective synthesis of l-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase

Cited by 19 publications

References 27 publications

Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library

Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library

Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids

Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine

Contact Info

Product

Resources

About