Biosynthesis and biotechnological application of non-canonical amino acids: Complex and unclear

Zou, Huibin; Li, Lei; Zhang, Tongtong; Shi, Mengxun; Zhang, Nan; Huang, Jinbo; Xian, Ming

doi:10.1016/j.biotechadv.2018.07.008

Cited by 27 publications

(12 citation statements)

References 130 publications

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“…Non-proteinogenic amino acids may have diverse physiological functions, for example, regulatory functions in metabolic cycles [ 5 ], or anti-bacterial, anti-inflammatory, anti-tumor and anti-hypertensive effects. Extensive reviews have already been published on these aspects [ 6 , 7 , 8 ]. The properties of halogenated antimicrobial peptides (AMPs), both native and synthetic, and their possible contribution to the growing problem of antibiotic resistance are also considered.…”

Section: Introductionmentioning

confidence: 99%

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Mardirossian

Rubini

Adamo³

et al. 2021

Molecules

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The 3D structure and surface characteristics of proteins and peptides are crucial for interactions with receptors or ligands and can be modified to some extent to modulate their biological roles and pharmacological activities. The introduction of halogen atoms on the side-chains of amino acids is a powerful tool for effecting this type of tuning, influencing both the physico-chemical and structural properties of the modified polypeptides, helping to first dissect and then rationally modify features that affect their mode of action. This review provides examples of the influence of different types of halogenation in amino acids that replace native residues in proteins and peptides. Examples of synthetic strategies for obtaining halogenated amino acids are also provided, focusing on some representative compounds and their biological effects. The role of halogenation in native and designed antimicrobial peptides (AMPs) and their mimetics is then discussed. These are in the spotlight for the development of new antimicrobial drugs to counter the rise of antibiotic-resistant pathogens. AMPs represent an interesting model to study the role that natural halogenation has on their mode of action and also to understand how artificially halogenated residues can be used to rationally modify and optimize AMPs for pharmaceutical purposes.

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Section: Introductionmentioning

confidence: 99%

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Mardirossian

Rubini

Adamo³

et al. 2021

Molecules

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“…Incorporation into proteins for electron paramagnetic resonance spectroscopy Widder et al, 2019 (Continued) Herger et al, 2016;Romney et al, 2017;Boville et al, 2018a,b;Dick et al, 2019 Metal-chelating NcAAs for metalloprotein engineering e.g., (2,2 -bipyridyn-5-yl)alanine and 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid Almhjell and Mills, 2018 Further NcAAs can be consulted in Blaskovich (2016), Zou et al (2018), Narancic et al (2019), and Hedges and Ryan (2020).…”

Section: Patel 2001mentioning

confidence: 99%

“…The occurrence and biological activity of NcAAs in vivo is hugely diverse, and some of their properties have been reflected in different papers (Wagner and Musso, 1983;Hunt, 1985;Nunn et al, 2010;Yamane et al, 2010;Walsh et al, 2013;Blaskovich, 2016;Zou et al, 2018;Narancic et al, 2019;Hedges and Ryan, 2020). Broadly, several NcAAs are utilized as intermediates in primary metabolic pathways (e.g., homoserine, ornithine, citrulline,.…”

Section: Introductionmentioning

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.

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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.

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“…Given the apparent advantages in terms of selectivity, sustainability, and evolvability, biocatalytic preparation of ncAAs has attracted increasing interest 9,10 . From a retrosynthetic perspective, the utilization of coupling reactions imparts excellent bene ts as it introduces quite a few atom economical reactions that allow multistep procedures and puri cations to be avoided to provide a target product 11 .…”

Section: Introductionmentioning

confidence: 99%

Development of a versatile and efficient C–N lyase platform for asymmetric hydroamination via computational enzyme redesign

et al. 2021

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Although C-N bonds are ubiquitous in natural products, pharmaceuticals, and agrochemicals, biocatalysts that forge these bonds with high atom e ciency and enantioselectivity have primarily been limited to a few select enzymes. In particular, the use of ammonia lyases has emerged as a powerful strategy to access C-N bond formation through hydroamination reactions, which has no counterpart in traditional synthetic chemistry. However, the broad utility of ammonia lyases is rather restricted due to their narrow synthetic scope, and the conjugate addition of a matrix of nucleophilic donors to electrophilic acceptors remains a longstanding challenge. Herein, we report the computational redesign of aspartase, a highly speci c ammonia lyase, to yield C-N lyases with unprecedented cross-compatibility of nonnative nucleophiles and electrophiles. A wide range of noncanonical amino acids (ncAAs) are afforded with excellent conversion (up to 99%), regioselectivity > 99%, and product enantiomeric excess > 99%, and the process is scalable under industrially relevant protocols (demonstrated in kilogram-scale synthesis). Furthermore, the redesigned enzymes can be facilely integrated in cascade reactions, as we demonstrated the synthesis of β-lactams with different substitution patterns at the N-1 and C-4 positions in a one-pot reaction. This versatile and e cient C-N lyase platform supports the preparation of diverse libraries of ncAAs and their derivatives and will present opportunities in medicinal chemistry and synthetic biology.

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Biosynthesis and biotechnological application of non-canonical amino acids: Complex and unclear

Cited by 27 publications

References 130 publications

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

Natural and Synthetic Halogenated Amino Acids—Structural and Bioactive Features in Antimicrobial Peptides and Peptidomimetics

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

Development of a versatile and efficient C–N lyase platform for asymmetric hydroamination via computational enzyme redesign

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