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An Overview on D-Amino Acids

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An Overview on D-Amino Acids Amino Acids DOI 10.1007/s00726-017-2459-5 REVIEW ARTICLE An overview on d‑amino acids Giuseppe Genchi1 Received: 19 April 2017 / Accepted: 26 June 2017 © Springer-Verlag GmbH Austria 2017 Abstract More than half a century ago researchers thought Keywords D-amino acid · Amino acid racemase · D-amino that D-amino acids had a minor function compared to acid oxidase · D-Asp · D-Ser L-enantiomers in biological processes. Many evidences have shown that D-amino acids are present in high concen- tration in microorganisms, plants, mammals and humans Introduction and fulfl specifc biological functions. In the brain of mam- mals, D-serine (D-Ser) acts as a co-agonist of the N-methyl- Proteins are the most abundant biological macromolecules D-aspartate (NMDA)-type glutamate receptors, responsible occurring in all cells and all parts of cells. All proteins, both for learning, memory and behaviour. D-Ser metabolism is from bacteria and from the most complex forms of life, are relevant for disorders associated with an altered function of composed of 20 amino acids, covalently linked through the NMDA receptor, such as schizophrenia, ischemia, epi- a peptide bond in a myriad of different combinations and lepsy and neurodegenerative disorders. On the other hand, sequences. From these 20 building blocks, all organisms can D-aspartate (D-Asp) is one of the major regulators of adult turn out different products such as enzymes, hormones, trans- neurogenesis and plays an important role in the develop- porters, antibodies, lens proteins, haemoglobin transporting ment of endocrine function. D-Asp is present in the neu- oxygen, cytochromes transporting electrons, antibiotics and a roendocrine and endocrine tissues and testes, and regulates myriad of other substances with distinct biological activities. the synthesis and secretion of hormones and spermatogen- All 20 standard amino acids found in proteins are esis. Also food proteins contain D-amino acids that are nat- α-amino acids, i.e. the general structure of the amino urally originated or processing-induced under conditions acids includes a carboxyl group and an amino group, both such as high temperatures, acid and alkali treatments and bonded to the α-carbon atom (the one next to the carboxyl fermentation processes. The presence of D-amino acids in group); this α-carbon is also linked both to a hydrogen and dairy products denotes thermal and alkaline treatments and to a side chain group. microbial contamination. Two enzymes are involved in the There are about 500 amino acids in nature, but only 20 metabolism of D-amino acids: amino acid racemase in the are proteogenic. Proteins are synthetized on polysomes in the synthesis and D-amino acid oxidase in the degradation. presence of mRNA, rRNA and tRNA as simple amino acid chains. Protein synthesis ends by a termination codon in the mRNA. To achieve its biologically active form, the new poly- peptide must fold into its proper three-dimensional confor- mation after posttranslational reactions. The new polypeptide Handling Editor: J. D. Wade. can undergo enzymatic reaction, including the formation of * Giuseppe Genchi disulfde bridges; addition of methyl, carboxyl, acetyl, phos- [email protected] phoryl, palmitoyl, retinoyl, or other groups to some amino acid residues; proteolytic cleavage; attachment of oligosaccharides 1 Dipartimento di Farmacia e Scienze della Salute e della Nutrizione, Università della Calabria (UNICAL), Arcavacata or prosthetic groups. Amino terminus may be blocked, and dif- di Rende, Cosenza 87036, Italy ferent moieties, small and large, can be added to the reactive 1 3 G. Genchi groups of proteins with covalent modifcation reactions. As a Special nomenclature has been employed to specify the result of carbohydrates addition, biophysical properties as well absolute confgurations of the four substituents of asym- as biological activities and stability increase, interaction with metric carbon atoms. The absolute confgurations of simple membrane receptors or nucleic acids can change and enzymes sugar and amino acids are specifed by the L- and D-systems catalytic properties can depend on side chain modifcation. based on the absolute confguration proposed by Emil Fis- Besides, the reversible phosphorylation of serine, threonine cher (1891) of the three-carbon atom glyceraldehyde, the and tyrosine (Burnett and Kennedy 1954) is greatly important smallest sugar to have an asymmetric carbon atom. For for the entire network of intracellular signalling. A new type all chiral compounds, stereoisomers with a confguration of posttranslational reaction has been revealed about 50 years related to that of L-glyceraldehyde are designated L, while ago, i.e. the conversion of certain amino acids in peptides or stereoisomers related to D-glyceraldehyde are designated proteins from the L- to the D-confguration (Bevins and Zasloff D. 1990; Kreil 1997). According to the convention of E. Fischer, the mol- ecule of glyceraldehyde is written (with respect to the chiral carbon atom) with aldehyde group (–CHO) upward Stereochemistry of α‑amino acids and methyl group (–CH3) downwards. The –OH group on the chiral carbon is left in the L-stereoisomer and right in Every object has a mirror image and the elements of the pair the D-stereoisomer (Fig. 1). The amino acid alanine will of objects, that are mirror images, can be superimposed on be written with the carboxyl group (–COOH) upward, and each other. In other cases, the mirror image objects cannot the methyl group (–CH3) downward. The –NH2 group on be superimposed on each other, but are related to each other the chiral carbon is toward the left in the L-stereoisomer as the right hand is to the left hand. Such not-superimpos- and to the right in the D-stereoisomer (Fig. 1). It is impor- able mirror images are said to be chiral (from the classic tant to note that not all L-amino acids are L levorotary Greek “χειρ”, hand). Frequently a chiral centre in biomole- (rotating plane-polarized light to the left), but they can cules is a carbon atom (sp 3 hybridized) linked to four differ- rotate the plane of polarized light to the right; and in the ent substituents. For all standard amino acids, the α-carbon same way not all D-amino acids are D dextrorotary (rotat- is bonded to four different groups: a carboxyl group (– ing plane-polarized light to the right), but they can rotate COOH), an amine group (–NH2), a hydrogen (–H) and a the plane of polarized light to the left. By E. Fischer’s side chain R group. Glycine has on α-carbon two hydrogen atoms; therefore, only glycine does not have a chiral centre. Because of the tetrahedral nature of sp3 orbitals of the carbon atom, the four different substituent groups can occupy two different spatial arrangements that are not superimposable mirror images to each other. These two forms, called enantiomers, represent a new class of ste- reoisomers. Isoleucine and threonine have four stereoi- somers, because these amino acids have a second stereo- genic centre in their β-carbon atom. All molecules with a chiral centre are optically active and can rotate the plane- polarized light, when examined in a polarimeter. Optical activity is given by all compounds existing in two forms, whose structures are not superimposable mirror images to each other. This condition is met by compounds contain- ing one (or more) asymmetric tetrahedral carbon atom(s), i.e. carbon atom(s) with four different substituents. The substances that rotate clockwise (to the right) to the plane of polarized light are said to be dextrorotatory (from the Latin “dexter”, right), while those that rotate counter- clockwise to (to the left) the plane of polarized light are said to be levorotatory (from the Latin “laevus”, left). In general, D- and L-stereoisomers (enantiomers) have the same chemical and physical properties, with the excep- tion of the rotation of the plane of polarized light in dif- Fig. 1 Relationship of stereoisomers of alanine with the absolute ferent directions, i.e. dextrorotatory or levorotatory. confguration of L- and D-glyceraldehyde 1 3 An overview on D-amino acids convention, L and D refer only the absolute confguration bacterial activity produce high quantity of D-Ala in fruit of the four substituents around the chiral atom. juices (Gandolf et al. 1994). The observation by several authors that processed commercial foods contained various D-amino acids has prompted numerous studies investigating the presence of d‑Amino acids of dietary origin D-amino acids in a variety of foods. Gobbetti et al. (1994) found that the use of lactic acid and yeast in the fermen- Food proteins usually contain L-α-amino acids, but some tation of sourdough before baking results in the produc- D-isomers occur in food either naturally originated or tion of free D-Ala and D-Glu in the dough. processing-induced under specifc conditions such as In ewes’ and cows’ milk, D-amino acids originated from high temperatures, strong acid and alkali treatments, enzymatic digestion of peptides and proteins containing fermentation processes or cases of non-fermented foods D-amino acids derived from peptidoglycan proteins of adulteration (Hayase et al. 1975; Friedman et al. 1984; microbial cell walls in the ruminants’ rumen. In fact, milk Chiavaro et al. 1998). from cows, goats and ewes, but not human milk, con- Food stores prepare and sell increasing quantities of tains free D-Ala, D-Asp, D-Glu, D-Ser and D-lysine (D-Lys) foods (baked potatoes, fruit juices and fruit pulp, break- (Albert et al. 2007). In addition, these same amino acids fast cereals, tomato sauces, milk, etc.), which in some are present in daily consumed ripened cheeses, and the cases contain substantial quantities of D-amino acids D-amino acid content varies among cheeses and changes (Csapò et al.
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