Highly efficient preparation of active S-phenyl-L-cysteine with tryptophan synthase using a chemoenzymatic method

Xu, Lisheng; Zhang, Xingtao; Gao, Guizhen; Sun, Yue

doi:10.1186/s12896-019-0538-2

Cited by 5 publications

(4 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Trans-4-Hydroxy-L-proline Chiral synthon for the chemical synthesis for pharmaceuticals such as antiphlogistics, carbapenems and ACE-inhibitors Taste-enhancing properties and probable health benefits, approved as GRAS ingredient by the FDA. Mu et al, 2015Mu et al, , 2019Yang et al, 2020 18 F-and 11 C -labeled NcAAs Preclinical and clinical tumor PET/CT imaging Sun et al, 2018 α-Vinylic AAs L-Vinylglycine, useful for the study of PLP-dependent enzymes Berkowitz et al, 2006 L-Cys derivatives L-ethionine, S-phenyl-L-cysteine, potential applicability as an antiretroviral/protease inhibitor for HIV Xu et al, 2019;Yu et al, 2019 L-pHFG and derivatives Found in several peptidic natural products including the vancomycin group of antibiotics (e.g., vancomycin, chloroeremomycin, and complestatin) as well as other antimicrobial compounds such as ramoplanin Al Toma et al, 2015 Fluorinated amino acids Different applications in medicinal chemistry (e.g., amino acid decarboxylase inhibitors, bioisosteres, building block for different drugs, . .…”

Section: Patel 2001mentioning

confidence: 99%

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

Section: Patel 2001mentioning

confidence: 99%

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

show abstract

“…Directed evolution can promote the enzymatic activity of lipase, xylanase, a-galactosidases, monoamine oxidase and nitrilase [14][15][16][17][18][19]. L-tryptophan and S-phenyl-L-cysteine were synthesized by tryptophan synthase of Escherichia coli k-12, and it was found that tryptophan synthase has the potential to synthesize L-tryptophan and its derivatives [20][21][22]. In this study, directed evolution of tryptophan synthase was performed by error-prone PCR.…”

Section: Introductionmentioning

confidence: 99%

Directed Evolution Improves the Enzymatic Synthesis of L-5-Hydroxytryptophan by an Engineered Tryptophan Synthase

Huo

et al. 2021

Appl Biochem Biotechnol

Self Cite

View full text Add to dashboard Cite

L-5-Hydroxytryptophan is an important amino acid that is widely used in food and medicine. In this study, L-5-hydroxytryptophan was synthesized by a modi ed tryptophan synthase. A direct evolution strategy was applied to engineer tryptophan synthase from Escherichia coli to improve the e ciency of L-5hydroxytryptophan synthesis. Tryptophan synthase was modi ed by error-prone PCR. A high activity mutant enzyme (V231A/K382G) was obtained by a high-throughput screening method. The activity of mutant enzyme (V231A/K382G) is 3.79 times higher than that of its parent, and k cat /K m of the mutant enzyme (V231A/K382G) was 4.36 mM − 1 •s − 1 . The mutant enzyme (V231A/K382G) reaction conditions for the production of L-5-hydroxytryptophan were 100 mmol/L L-serine at pH 8.5 and 35°C for 15 h, reaching a yield of L-5-hydroxytryptophan of 86.7%. Directed evolution is an effective strategy to increase the activity of tryptophan synthase.

show abstract

Section: Introductionmentioning

confidence: 99%

Directed evolution improves the enzymatic synthesis of L-5-hydroxytryptophan by an engineered tryptophan synthase

Xu¹,

Li²,

Huo³

et al. 2021

Preprint

View full text Add to dashboard Cite

L-5-Hydroxytryptophan is an important amino acid that is widely used in food and medicine. In this study, L-5-hydroxytryptophan was synthesized by a modified tryptophan synthase. A direct evolution strategy was applied to engineer tryptophan synthase from Escherichia coli to improve the efficiency of L-5-hydroxytryptophan synthesis. Tryptophan synthase was modified by error-prone PCR. A high activity mutant enzyme (V231A/K382G) was obtained by a high-throughput screening method. The activity of mutant enzyme (V231A/K382G) is 3.79 times higher than that of its parent, and kcat/Km of the mutant enzyme (V231A/K382G) was 4.36 mM− 1∙s− 1. The mutant enzyme (V231A/K382G) reaction conditions for the production of L-5-hydroxytryptophan were 100 mmol/L L-serine at pH 8.5 and 35°C for 15 h, reaching a yield of L-5-hydroxytryptophan of 86.7%. Directed evolution is an effective strategy to increase the activity of tryptophan synthase.

show abstract

Highly efficient preparation of active S-phenyl-L-cysteine with tryptophan synthase using a chemoenzymatic method

Cited by 5 publications

References 13 publications

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

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

Directed Evolution Improves the Enzymatic Synthesis of L-5-Hydroxytryptophan by an Engineered Tryptophan Synthase

Directed evolution improves the enzymatic synthesis of L-5-hydroxytryptophan by an engineered tryptophan synthase

Contact Info

Product

Resources

About