Natural Occurrence and Industrial Applications of d‐Amino Acids: An Overview

Abstract

Interest in D-amino acids has increased in recent decades with the development of new analytical methods highlighting their presence in all kingdoms of life. Their involvement in physiological functions, and the presence of metabolic routes for their synthesis and degradation have been shown. Furthermore, D-amino acids are gaining considerable importance in the pharmaceutical industry. The immense amount of information scattered throughout the literature makes it difficult to achieve a general overview of their applications. This review summarizes the state-of-the-art on D-amino acid applications and occurrence, providing both established and neophyte researchers with a comprehensive introduction to this topic.

Formyl Peptide Receptors from Immune and Vomeronasal System Exhibit Distinct Agonist Properties

“…A particularly interesting feature of mFpr-rs1 is its strong stereo-selective preference for peptides with a d -amino acid in the last C-terminal position. This finding is rather surprising because d -amino acids are relatively rare in nature, and most natural proteins and peptides consist solely of l -amino acids (38). However, microorganisms are a potent natural source for d -amino acid-containing peptides, as these are found in the bacterial cell wall and in toxins secreted by fungi (38).…”

Differential acquisition of amino acid and peptide enantiomers within the soil microbial community and its implications for carbon and nitrogen cycling in soil

“…As D-isomers are prevalent within the bacterial cell wall (Roberts et al, 2009), and can contain D-peptides up to three amino acids in length (Schleifer and Kandler, 1972), it may provide bacteria with an exclusive, selfcycling mechanism that excludes competition by fungi and plants. This source of N may be a significant pool, with bacteria being shown to be capable of assimilating exogenous sources of Damino acid and incorporating them into peptidoglycan (Lam et al, 2009), as well as demonstrating pathways for their conversion into more metabolically available forms (Yonaha et al, 1975;Inagaki et al, 1986;Martinez-Rodriguez et al, 2010).…”

Rational re-design of the “double-racemase hydantoinase process” for optically pure production of natural and non-natural l-amino acids

“…However, from the practical point of view, hydantoinases have been classified into d-, l-and non-selective, depending on their enantioselectivity [16]. Due to the importance of d-amino acids as intermediates for the production of sweeteners, pesticides and other active compounds [17], and the fact that most reported hydantoinases were d-enantioselective [16], the "hydantoinase process" has mainly been employed for the production of d-amino acids [18]. Our group has developed biocatalytic systems overexpressing d-hydantoinase, d-carbamoylase and hydantoin racemase for optically pure d-amino acid production [19,20].…”