Formation Of Serine Research Articles

384 Synthesis of glycine from trans-4-hydroxy-L-proline by placentae but not endometria of gestating gilts

Abstract Trans-4-hydroxy-L-proline (Hyp) is an abundant amino acid in the collagen of pigs. The turnover of this protein releases a large amount of Hyp, traditionally considered a metabolic waste. However, results of recent studies documented the conversion of Hyp into glycine in young pigs. Because pregnant gilts are typically fed a soybean meal-based diet that contains insufficient glycine and provides only 35% of the total glycine needed by pregnant gilts, it is possible that the conceptus can form glycine from Hyp. This hypothesis was tested in the present study. Gilts were fed a 1.8-kg corn- and soybean meal-based diet containing 14% crude protein. On d 90 of gestation, gilts (n = 5) were hysterectomized after euthanasia. Slices (~ 100 mg) of placentae or endometria were incubated at 37 °C for 2 h in oxygenated (95% O2/5% CO2) Krebs-Henseleit bicarbonate buffer (pH 7.4, with 5 mM D-glucose) containing 0 or 2 mM Hyp. After a period of 2 h incubation, 200 μL of 1.5 M HClO4 was added into the incubation medium to stop the reaction. The tissues were homogenized and rinsed with 1 mL water, followed by the addition of 100 μL of 2 M K2CO3. The neutralized extract was analyzed for amino acids using HPLC involving derivatization with o-phthaldialdehyde. Tissues that received no incubation time were determined as well. Data were analyzed by the paired t-test. Results indicated that glycine was produced from 2 mM Hyp by the placenta (Table 1). Glycine was subsequently converted into serine by the placenta. The formation of glycine and serine from Hyp was not due to protein breakdown because there were no differences (P > 0.05) in concentrations of tyrosine (an amino acid that is neither synthesized nor degraded by porcine placentae) in the incubation medium plus tissue at the end of a 2-h incubation period. In contrast to placentae, endometria did not form glycine or serine from Hyp. These findings indicate an important role for Hyp in the provision of both glycine and serine in the conceptus, which may be nutritionally and physiologically significant to compensate for a deficiency of glycine in maternal diets for gestating gilts. (Supported by a USDA/NIFA grant # 2022-67015-36376 and USDA multistate Hatch project #7752: S1081)

Cryogenic gastronomy at The Restaurant at the End of the Universe – exploring interstellar serine synthesis from α-glycyl radical and other ingredients

Amino acids are essential for Earth-like life and are hypothesised to have originated in interstellar space, potentially being transported to Earth via meteorite impacts. Detecting amino acids in interstellar environments and understanding their formation mechanisms through laboratory experiments are crucial for supporting this hypothesis and unravelling the origins of life. In this study, the formation of serine ( NH 2 CH ( CH 2 OH ) COOH ) from α-glycyl ( NH 2 C ⋅ HCOOH ) and hydroxymethyl ( ⋅ CH 2 OH ) radicals was investigated using quantum chemical computations. It was found that the anticipated recombination reaction, along with analogous formation pathways of other natural amino acids, is accompanied by competing reactions yielding alternative products, potentially diminishing serine formation. Alternative interstellar formation pathways for serine are proposed, which could be experimentally tested by future laboratory studies.

Genome-scale metabolic model led engineering of Nothapodytes nimmoniana plant cells for high camptothecin production.

Camptothecin (CPT) is a vital monoterpene indole alkaloid used in anti-cancer therapeutics. It is primarily derived from Camptotheca acuminata and Nothapodytes nimmoniana plants that are indigenous to Southeast Asia. Plants have intricate metabolic networks and use them to produce secondary metabolites such as CPT, which is a prerequisite for rational metabolic engineering design to optimize their production. By reconstructing metabolic models, we can predict plant metabolic behavior, facilitating the selection of suitable approaches and saving time, cost, and energy, over traditional hit and trial experimental approaches. In this study, we reconstructed a genome-scale metabolic model for N. nimmoniana (NothaGEM iSM1809) and curated it using experimentally obtained biochemical data. We also used in silico tools to identify and rank suitable enzyme targets for overexpression and knockout to maximize camptothecin production. The predicted over-expression targets encompass enzymes involved in the camptothecin biosynthesis pathway, including strictosidine synthase and geraniol 10-hydroxylase, as well as targets related to plant metabolism, such as amino acid biosynthesis and the tricarboxylic acid cycle. The top-ranked knockout targets included reactions responsible for the formation of folates and serine, as well as the conversion of acetyl CoA and oxaloacetate to malate and citrate. One of the top-ranked overexpression targets, strictosidine synthase, was chosen to generate metabolically engineered cell lines of N. nimmoniana using Agrobacterium tumefaciens-mediated transformation. The transformed cell line showed a 5-fold increase in camptothecin production, with a yield of up to 5 µg g-1.

Syntone Chemistry. Theoretical study on the formation of glycine, alannine and serine

Three synthons: methylene, nitrene and carbon monoxide form aziridinone in the presence of molecular nitrogen at low temperatures. This one, in contact with the same three synthons could form the precursors of the first proteinogenic amino acids. This paper is a theoretical, thermodynamically and reactivity study concerning the formation of the three previously named amino acids at low temperature conditions. The key intermediates are identified in the formation of the three amino acids: aziridinone, aziridinonil and methyl-aziridinonil radicals. The quantitative results, enthalpies of formation, reaction enthalpies and free energies were taken from quantum mechanical calculations acquired by density functional method (DFT): B88-LYP.

The Glycerate and Phosphorylated Pathways of Serine Synthesis in Plants: The Branches of Plant Glycolysis Linking Carbon and Nitrogen Metabolism.

Serine metabolism in plants has been studied mostly in relation to photorespiration where serine is formed from two molecules of glycine. However, two other pathways of serine formation operate in plants and represent the branches of glycolysis diverging at the level of 3-phosphoglyceric acid. One branch (the glycerate – serine pathway) is initiated in the cytosol and involves glycerate formation from 3-phosphoglycerate, while the other (the phosphorylated serine pathway) operates in plastids and forms phosphohydroxypyruvate as an intermediate. Serine formed in these pathways becomes a precursor of glycine, formate and glycolate accumulating in stress conditions. The pathways can be linked to GABA shunt via transamination reactions and via participation of the same reductase for both glyoxylate and succinic semialdehyde. In this review paper we present a hypothesis of the regulation of redox balance in stressed plant cells via participation of the reactions associated with glycerate and phosphorylated serine pathways. We consider these pathways as important processes linking carbon and nitrogen metabolism and maintaining cellular redox and energy levels in stress conditions.

The In Vitro Redundant Enzymes PurN and PurT Are Both Essential for Systemic Infection of Mice in Salmonella enterica Serovar Typhimurium.

Metabolic enzymes show a high degree of redundancy, and for that reason they are generally ignored in searches for novel targets for anti-infective substances. The enzymes PurN and PurT are redundant in vitro in Salmonella enterica serovar Typhimurium, in which they perform the third step of purine synthesis. Surprisingly, the results of the current study demonstrated that single-gene deletions of each of the genes encoding these enzymes caused attenuation (competitive infection indexes [CI] of <0.03) in mouse infections. While the ΔpurT mutant multiplied as fast as the wild-type strain in cultured J774A.1 macrophages, net multiplication of the ΔpurN mutant was reduced approximately 50% in 20 h. The attenuation of the ΔpurT mutant was abolished by simultaneous removal of the enzyme PurU, responsible for the formation of formate, indicating that the attenuation was related to formate accumulation or wasteful consumption of formyl tetrahydrofolate by PurU. In the process of further characterization, we disclosed that the glycine cleavage system (GCV) was the most important for formation of C1 units in vivo (CI = 0.03 ± 0.03). In contrast, GlyA was the only important enzyme for the formation of C1 units in vitro The results with the ΔgcvT mutant further revealed that formation of serine by SerA and further conversion of serine into C1 units and glycine by GlyA were not sufficient to ensure C1 formation in S Typhimurium in vivo The results of the present study call for reinvestigations of the concept of metabolic redundancy in S Typhimurium in vivo.

Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase.

In bacteria, cysteine can be synthesized from serine by two steps involving an L-serine O-acetyltransferase (SAT) and a cysteine synthase (CysK). While CysK is found in the publicly available annotated genome from Lactobacillus casei ATCC 334, a gene encoding SAT (cysE) is missing. In this study, we found that various strains of L. casei grew in a chemically defined medium containing sulfide as the sole sulfur source, indicating the presence of a serine O-acetyltransferase. The gene lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). To study the function of this gene, it was cloned from L. casei FAM18110. The purified, recombinant protein did not acylate L-homoserine in vitro. Instead, it catalyzed the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the L. casei gene complemented an Escherichia coli cysE mutant strain but not an E. coli metA mutant. This clearly demonstrated that the gene annotated as metA in fact encodes the SAT function and should be annotated as cysE.

Amino Acid Metaclusters: Implications of Growth Trends on Peptide Self-Assembly and Structure.

Ion-mobility mass spectrometry is utilized to examine the metacluster formation of serine, asparagine, isoleucine, and tryptophan. These amino acids are representative of different classes of noncharged amino acids. We show that they can form relatively large metaclusters in solution that are difficult or impossible to observe by traditional solution techniques. We further demonstrate, as an example, that the formation of Ser metaclusters is not an ESI artifact because large metaclusters can be detected in negative polarity and low concentration with similar cross sections to those measured in positive polarity and higher concentration. The growth trends of tryptophan and isoleucine metaclusters, along with serine, asparagine, and the previously studied phenylalanine, are balanced among various intrinsic properties of individual amino acids (e.g., hydrophobicity, size, and shape). The metacluster cross sections of hydrophilic residues (Ser, Asn, Trp) tend to stay on or fall below the isotropic model trend lines whereas those of hydrophobic amino acids (Ile, Phe) deviate positively from the isotropic trend lines. The growth trends correlate well to the predicted aggregation propensity of individual amino acids. From the metacluster data, we introduce a novel approach to score and predict aggregation propensity of peptides, which can offer a significant improvement over the existing methods in terms of accuracy. Using a set of hexapeptides, we show that the strong negative deviations of Ser metaclusters from the isotropic model leads a prediction of microcrystalline formation for the SFSFSF peptide, whereas the strong positive deviation of Ile leads to prediction or fibril formation for the NININI peptide. Both predictions are confirmed experimentally using ion mobility and TEM measurements. The peptide SISISI is predicted to only weakly aggregate, a prediction confirmed by TEM.

Quantum-chemical approach to serine formation in the interstellar medium: A possible reaction pathway

Radical-radical and radical-neutral interaction schemes are very important for the formation of comparatively complex molecules in low-temperature chemistry. The formation of amino acids, such as serine, in the interstellar medium is quite difficult. We explored the possibility of serine formation in the interstellar medium through detected interstellar molecules such as CH, CO, and OH by radicalradical and radical-neutral interactions in the gaseous phase using rigorous quantum-chemical calculations. The reaction energies, the low potential barrier and the structures of all the geometries involved in the reaction path show that serine formation is possible in interstellar space via the reaction paths.

Cytochrome P450 1A1 and Glutathione S-Transferase Pi 1 Mutations in Pharyngeal and Laryngeal Carcinoma

In the current case control study, 94 pharyngeal, 67 laryngeal cancer cases and 150 cancer free controls were screened via PCR-SSCP assay. Mean ages of pharyngeal, laryngeal cancer patients and control was 48.14 (± 16.7), 48.56 (± 17.4) and 46 (± 17.69) years respectively. Results revealed two novel mutations in CYP1A1 gene, a substitution mutation of A2842C resulting in missense tyrosine to serine formation and frameshift mutation due to insertion of thymidine at nucleotide 2842 resulting in 495 nucleotide sequences to alter. It was found that 3.2% pharyngeal and 2.98% laryngeal cancer patients had these mutations in CYP1A1. In GSTP1 gene exon 7, an A2848T substitution causes a leucine to leucine formation whereas G2849A substitution causes alanine to threonine formation at amino acid 166 and 167 respectively. These exonic mutations were found in 7.4% pharyngeal cancer and 9% laryngeal cancer patients. Two intronic deletions of C at nucleotide 1074 and 1466 were found in 1% pharyngeal and laryngeal cancer patients. Accumulation of mutations in CYP1A1 and GSTP1 genes seem to be associated with increased risk of pharyngeal and laryngeal cancer development.

Acetonitrile: A Plausible Source of Amino Acids on the Primitive Earth.

Synthesis of amino acids from aqueous solution of acetonitrile has been carried out by the action of heat.and revealed the formation of lysine, aspartic acid, serine, glycine ,glutamic acid, alanine, valine and leucine. Amino acid synthesis was accelerated in the presence of copper exchanged montmorillonite clay followed by calcium and magnesium exchanged clays. Synthesis of important biomolecules from aqueous solution of acetonitrile may throw some light on the process of chemical evolution.

Comparative proteomic analysis revealed metabolic changes and the translational regulation of Cry protein synthesis in Bacillus thuringiensis

B. thuringiensis strain YBT-1520 is highly toxic to some Lepidopteran pests and is used to control pests in southern part of China. The aim of this work is to uncover the metabolic changes associated with the ICP synthesis. A comparative proteomic analysis on the strain was performed with 2-DE and MALDI-TOF-MS methods with the bacterial culture grown in a modified defined minimal medium. Transcriptional expression of some key enzymes for carbohydrate metabolism was also investigated with qPCR. Seventy-two proteins differentially expressed at least two folds were identified. Significant changes were observed in metabolisms when comparing stationary growth phase to mid-log phase. In late-stationary phase, five major phenomena were observed: 1) the glycolysis cycle was redirected into pentose phosphate pathway and ended in serine formation; 2) the tricarboxylic acid (TCA) cycle was suppressed; 3) poly(3-hydroxybutyrate) (PHB) was considered to be the important energy and carbon supply; 4) collectively increased proteases suggested massive protein degradation to release amino acids, and 5) translation-related factors were up-regulated including EF-Tu, GroEL and GatB, while the negative regulator YfiA was down. The metabolic changes of bacterium during growth shift indicated that the cells acquired energy, amino acid precursors and translation-related factors for the ICP synthesis.

A high-performance liquid chromatography-based fluorometric method for assaying serine hydroxymethyltransferase toward serine formation

A high-performance liquid chromatography (HPLC)-based fluorometric method for measuring serine hydroxymethyltransferase (SHMT) activity toward formation of serine and (6 S)-H 4PteGlu n has been developed. In this method, serine formed by SHMT activity is reacted with 4-fluoro-7-nitro-2,1,3-benzoxadiazole (NBD-F) to form the fluorescent adduct NBD–serine. The fluorescent assay components are then separated by reversed-phase chromatography, and NBD–serine is quantified by comparison with standards. This method was used to determine the K m and k cat values for 5,10-CH 2–H 4PteGlu 5 of an SHMT from Arabidopsis thaliana. These data represent the first determination of kinetic parameters for ( 6S)-5,10-CH 2–H 4PteGlu 5 for an SHMT from any organism.

Glycine oxidation and conversion into amino acids in Saccharomyces cerevisiae and Candida albicans

Humans are exposed much more often to exogenous Saccharomyces cerevisiae (a baker's yeast) than exogenous Candida albicans (a highly infectious yeast) but suffer no apparent complications from S. cerevisiae. We hypothesize that variations in characteristics between these two species may be due, in part, to differences in glycine metabolism. In this study, we examined differences in glycine oxidation between C. albicans and S. cerevisiae. Both C. albicans and S. cerevisiae were cultured in glycine enriched media, followed by determination of glycine oxidation and amino acid concentrations in cells. Glycine was degraded to a much greater extent in C. albicans than in S. cerevisiae. Threonine concentrations and glycine oxidation were also elevated in C. albicans. Almost all of the disappearance of glycine from incubation media was accounted for by the formation of serine, threonine, and CO(2) in S. cerevisiae, whereas these products represented only 50% of the metabolized glycine in C. albicans. The unidentified metabolites of glycine in C. albicans, presumably purines, could contribute to its infectious capacity and this warrants further study.

In vitro synthesis of arachidonoyl amino acids by cytochrome c

Arachidonoyl amino acids are a class of endogenous lipid messengers that are expressed in the mammalian central nervous system and peripherally. While several of their prominent pharmacologic effects have been documented, the mechanism by which arachidonoyl amino acids are biosynthesized has not been defined. We have previously observed that the mitochondrial protein, cytochrome c, is capable of catalyzing the formation of the prototypic arachidonoyl amino acid, arachidonoyl glycine, utilizing arachidonoyl CoA and glycine as substrates, in the presence of hydrogen peroxide. Here we report that cytochrome c is similarly able to catalyze the formation of N-arachidonoyl serine, N-arachidonoyl alanine, and N-arachidonoyl gamma aminobutyric acid from arachidonoyl CoA and the respective amino acids. The identities of the arachidonoyl amino acid products were verified by mass spectral fragmentation pattern analysis. The synthetic reactions exhibited Michaelis–Menten kinetics and continued favorably at physiologic temperature and pH. Spectral data indicate that both cytochrome c protein structure and a +3 heme iron oxidation state are required for the reaction mechanism to proceed optimally. Reactions designed to catalyze the formation of N-arachidonoyl dopamine were not efficient due to the rapid oxidation of dopamine substrate by hydrogen peroxide, consuming both reactants. Finally, under standard assay conditions, arachidonoyl CoA and ethanolamine were found to react spontaneously to form anandamide, independent of cytochrome c and hydrogen peroxide. Accordingly, it was not possible to demonstrate a potential role for cytochrome c in the biosynthetic mechanism for either arachidonoyl dopamine or anandamide. However, the ability of cytochrome c to effectively catalyze the formation of N-arachidonoyl serine, N-arachidonoyl alanine, and N-arachidonoyl gamma aminobutyric acid in vitro highlights its potential role for the generation of these lipid messengers in vivo.

Detection of Serine Octamer by Desorption Electrospray Ionization Mass Spectrometry in Resultant Mixture of Aspartic Acid Exposed to Sunshine Under Natural Conditions

Serine, one of the nonessential amino acids, is of principal interest because of its capability to form magic-number ionic clusters, which provide a remarkable preference for homochirality. With L-aspartic acid as the precursor, this study provides experimental evidence for serine formation in weak acidified aqueous solutions in the presence of iron, with exposure to sunlight, which simulates the natural conditions of the prebiotic aqueous environment. The resultant mixture is directly analyzed via desorption electrospray ionization mass spectrometry (DESI-MS), without any sample preseparation. The serine monomer is successfully detected as protonated molecules, giving a peak at m/z 106, which is confirmed by the MS/MS fragments. Protonated serine octamer (m/z 841) is also observed with significant abundance in the MS spectra and is confirmed by the MS/MS data, which shows the formation of the serine octamer by a synthesized serine in the resultant mixture. It is also found that the serine octamer yielded equivalent abundance in the DESI mass spectra in a wide pH range (pH = 1—5), and that existence of ferrous salt and sunshine are essential for the conversion of aspartic acid to serine in the acidic water solution.

Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution

BackgroundNon-ribosomal peptide synthetases (NRPSs) are large multimodular enzymes that synthesize a wide range of biologically active natural peptide compounds, of which many are pharmacologically important. Peptide bond formation is catalyzed by the Condensation (C) domain. Various functional subtypes of the C domain exist: An LCL domain catalyzes a peptide bond between two L-amino acids, a DCL domain links an L-amino acid to a growing peptide ending with a D-amino acid, a Starter C domain (first denominated and classified as a separate subtype here) acylates the first amino acid with a β-hydroxy-carboxylic acid (typically a β-hydroxyl fatty acid), and Heterocyclization (Cyc) domains catalyze both peptide bond formation and subsequent cyclization of cysteine, serine or threonine residues. The homologous Epimerization (E) domain flips the chirality of the last amino acid in the growing peptide; Dual E/C domains catalyze both epimerization and condensation.ResultsIn this paper, we report on the reconstruction of the phylogenetic relationship of NRPS C domain subtypes and analyze in detail the sequence motifs of recently discovered subtypes (Dual E/C, DCL and Starter domains) and their characteristic sequence differences, mutually and in comparison with LCL domains. Based on their phylogeny and the comparison of their sequence motifs, LCL and Starter domains appear to be more closely related to each other than to other subtypes, though pronounced differences in some segments of the protein account for the unequal donor substrates (amino vs. β-hydroxy-carboxylic acid). Furthermore, on the basis of phylogeny and the comparison of sequence motifs, we conclude that Dual E/C and DCL domains share a common ancestor. In the same way, the evolutionary origin of a C domain of unknown function in glycopeptide (GP) NRPSs can be determined to be an LCL domain. In the case of two GP C domains which are most similar to DCL but which have LCL activity, we postulate convergent evolution.ConclusionWe systematize all C domain subtypes including the novel Starter C domain. With our results, it will be easier to decide the subtype of unknown C domains as we provide profile Hidden Markov Models (pHMMs) for the sequence motifs as well as for the entire sequences. The determined specificity conferring positions will be helpful for the mutation of one subtype into another, e.g. turning DCL to LCL, which can be a useful step for obtaining novel products.

Quantification of pathways of glucose utilization and balance of energy metabolism of rabbit reticulocytes.

In this work it is demonstrated that glucose constitutes the main substrate of energy metabolism of rabbit reticulocytes under aerobic conditions in the presence of 5 mM glucose. Amino acids and fatty acids are minor sources of energy. The shares of processes utilizing glucose in reticulocytes were estimated from tracer experiments. A new mathematical technique used permits the derivation of closed terms for the specific radioactivity of single positions of C atoms of the metabolites of the citrate cycle. By means of regression analysis, the undetermined flux rates in the citrate cycle were calculated. On the basis of the data an overall balance sheet of glucose utilization and of ATP generation is given. About 45% of the glucose of reticulocytes is catabolized via the citrate cycle, about the same percentage yields lactate. Only 2% of the glucose was oxidized in the oxidative pentose pathway whereas the remainder is used for the formation of serine and glycine required for hemoglobin synthesis. These results are related to knowledge about the main processes utilizing ATP in reticulocytes, i.e. the synthesis of hemoglobin and the energy-dependent proteolysis. Our approach to the investigation of metabolic relations in the reticulocytes can be applied to other tissues in which equilibria between large metabolite pools play a role.

Radiation sensitivity, H2AX phosphorylation, and kinetics of repair of DNA strand breaks in irradiated cervical cancer cell lines.

Six human cervical cancer cell lines [five human papillomavirus (HPV) positive, one HPV negative] for induction and rejoining of DNA strand breaks and for kinetics of formation and loss of serine 139 phosphorylated histone H2AX (gammaH2AX). X-rays induced the same level of DNA breakage for all cell lines. By 8 hours after 20 Gy, <2% of the initial single-strand breaks remained and no double-strand breaks could be detected. In contrast, 24 hours after irradiation, gammaH2AX representing up to 30% of the initial signal still present. SW756 cells showed almost four times higher background levels of gammaH2AX and no residual gammaH2AX compared with the most radiosensitive HPV-negative C33A cells that showed the lowest background and retained 30% of the maximum level of gammaH2AX. Radiation sensitivity, measured as clonogenic-surviving fraction after 2 Gy, was correlated with the fraction of gammaH2AX remaining 24 hours after irradiation. A substantial correlation with gammaH2AX loss half-time measured over the first 4 hours was seen only when cervical cell lines were included in a larger series of p53-deficient cell lines. Interestingly, p53 wild-type cell lines consistently showed faster gammaH2AX loss half-times than p53-deficient cell lines. We conclude that cell line-dependent differences in loss of gammaH2AX after irradiation are related in part to intrinsic radiosensitivity. The possibility that the presence of gammaH2AX foci may not always signify the presence of a physical break, notably in some tumor cell lines, is also supported by these results.

Pathways to Glycine and Other Amino Acids in Ultraviolet-irradiated Astrophysical Ices Determined via Quantum Chemical Modeling

A recent experimental study reported that glycine and other amino acids were formed when cryogenic H2O ice containing small amounts of CH3OH, NH3, and HCN was subjected to ultraviolet (UV) irradiation. Quantum chemical calculations were employed to evaluate the viability of various pathways to the formation of glycine, alanine, and serine in dilute H2O ice containing CH3OH and HCN. Under the experimental processing conditions of deposition and UV irradiation at 15 K followed by heating to room temperature, amino acids can form by recombining radicals produced by dehydrogenating H2O and CH3OH and subsequently hydrogenating HCN. The study indicates that isotopic substitution experiments would identify CH3OH as the source of the C atom in the COOH carboxylic acid group of the amino acids observed in the irradiation experiments, with the CO+OH reaction playing an important role. The remaining C and N atoms in glycine are predicted to originate from HCN via sequential hydrogenation to yield CH2NH2. Formation pathways for alanine and serine are also discussed.