Formation Of Cysteine Research Articles

Colour formation of dihydroxyacetone with cysteine and its derivatives via Maillard reaction

Compared to the conventional solar tanning, sunless tanning has become the most popular way to obtain tanned skin due to convenience and safety. Dihydroxyacetone (DHA), a three-carbon sugar, is the main active ingredient in commercial sunless tanning products and its tanning chemistry is similar to the well-known Maillard reaction. Whereas most studies concerning sunless tanning reaction, over the past 60 years, have focused on the amino groups of amino acids, little information is available on the impact of thiol groups of cysteine on the colour formation with DHA. Hence, this study systematically investigated the colour formation of cysteine and DHA using a simplified model system at different molar ratios, reaction times, pH, and temperatures. The colour change and characteristics were quantitatively evaluated using colour difference (ΔE*) and CIE L*a*b* values, respectively. In addition, the reactivity of amino and thiol groups on the same cysteine with DHA was further investigated. It was found, for the first time, that the thiol group of cysteine significantly inhibited the colour formation with DHA, while its amino group has a strong colour-formation ability in anhydrous condition. This work not only presents a systematic study on the colour formation of cysteine with DHA and the role of its amino and thiol groups, but also provides new knowledge for understanding and controlling the colour formation of DHA tanning on human skin.

Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates.

Thiazolidine carboxylates such as thiazolidine-4-carboxylate (T4C) and thiazolidine-2-carboxylate (T2C) are naturally occurring sulfur analogues of proline. These compounds have been observed to have both beneficial and toxic effects in cells. Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde dehydrogenase (GSALDH) activities. PutA is shown here to catalyze the FAD-dependent PRODH oxidation of both T4C and T2C with catalytic efficiencies significantly higher than with proline. Stopped-flow experiments also demonstrate that l-T4C and l-T2C reduce PutA-bound FAD at rates faster than proline. Unlike proline, however, oxidation of T4C and T2C does not generate a substrate for NAD+-dependent GSALDH. Instead, PutA/PRODH oxidation of T4C leads to cysteine formation, whereas oxidation of T2C generates an apparently stable Δ4-thiazoline-2-carboxylate species. Our results provide new insights into the metabolism of T2C and T4C.

Colorimetric determination of cysteine and copper based on the peroxidase-like activity of Prussian blue nanocubes.

Prussian blue nanocubes were synthesized via a hydrothermal method. Significantly, the redox couple Ni3+/Ni2+ provided rich oxidation and reduction reactions, which enhance catalytic activity. Furthermore, PBNCs mimic peroxidase activity which could oxidise colourless tetramethyl benzidine (TMB) to a blue colour (TMB+) in the presence of H2O2. Thus, it can be used as a colorimetric sensing platform for detecting cysteine and Cu2+. The addition of cysteine to a TMB + PBNCs sensing system decreases the intensity of the blue colour in the solution with a decrease in the absorption peak at 652 nm in the UV visible spectrum. Subsequently, the addition of Cu2+ into the TMB + PBNCs + Cys sensing system increases the intensity of the blue colour due to complex formation of Cu and cysteine. Therefore, the change in intensity of the blue colour of TMB is directly proportional to the concentration of Cys and Cu2+. As a result, this sensing system is highly sensitive and selective with an effective low detection limit of 0.002 mM for cysteine and 0.0181 mM for Cu2+. Furthermore, this method was applied to the detection of cysteine and copper in spiked real samples and gave satisfactory results.

The impact of general anesthesia on methionine metabolism during cardiopulmonary bypass

It has been found out that methylation of nucleic acids, proteins and low-molecular substrates is necessary to renew cellular structures, their restoration and cytoprotection. Methionine plays the most important role in this process but whether its metabolism changes during anesthesia and how different anesthetics affect it, has not yet been studied. The objective : to study the metabolism of methionine during cardiopulmonary bypass when the direct myocardial revascularization is performed and the impact of the anesthetics used (propofol, desflurane, and sevoflurane) on methionine metabolism. Subjects and methods : 74 patients who underwent surgery due to coronary heart disease with cardiopulmonary bypass were enrolled in the study. The patients were divided into three groups by the anesthetic used (desflurane, sevoflurane, propofol). Levels of methionine, homocysteine, cysteine, and taurine were tested in the blood collected from veins and jugular vein before the aorta clamping and after the release of clamps. Results . In all three groups, lower levels of methionine and a higher level of homocysteine were observed after the release of clamps from the aorta, especially in the jugular vein. The most significant consumption of methionine was noted when propofol was used. In the same group, the exocytic release of homocysteine into the blood and the formation of cysteine were significantly lower. No significant difference was observed in the effect of desflurane and sevoflurane on methylation. Conclusion . During the anoxia, the consumption of methionine increases significantly but the intensity of demethylation/remethylation depends on the anesthetics used during anesthesia. The most significant decrease in the level of methionine as well as the remethylation of homocysteine into methionine occurs with the use of propofol, rather than inhalation anesthetics which may be a consequence of desflurane and sevoflurane cytoprotective properties.

Syntone Chemistry. Theoretical Study on the Formation of Cysteine, Aspartic Acid, Asparagine and Threonine

In this paper is presented a theoretical study of chemical reactivity on the formation of four proteinogenic amino acids: cysteine, aspartic acid, asparagine and threonine. According to a theoretical model based on three syntons: methylene, nitrene and carbon monoxide at low temperatures, aziridinone would be formed first. This one, with methylene and carbon monoxide forms further the precursors intermediates of these four proteinogenic amino acids. Finally, the precursors in reaction with water, a key component of the primary atmosphere, lead to amino acids specified above. The study is mainly based on quantum mechanical calculations, B88-LYP DFT. Methylaziridonil, aziridonilacetyl and ethylaziridonil radicals should be formed at low temperature, which finally in reaction with water will form cysteine, aspartic acid, asparagine and threonine.

Efficient production of glutathione with multi-pathway engineering in Corynebacterium glutamicum.

Glutathione is a bioactive tripeptide composed of glycine, L-cysteine, and L-glutamate, and has been widely used in pharmaceutical, food, and healthy products. The current metabolic studies of glutathione were mainly focused on the native producing strains with precursor amino acid supplementation. In the present work, Corynebacterium glutamicum, a workhorse for industrial production of a series of amino acids, was engineered to produce glutathione. First, the introduction of glutathione synthetase gene gshF from Streptococcus agalactiae fulfilled the ability of glutathione production in C. glutamicum and revealed that L-cysteine was the limiting factor. Then, considering the inherent capability of L-glutamate synthesis and the availability of external addition of low-cost glycine, L-cysteine biosynthesis was enhanced using a varieties of pathway engineering methods, such as disrupting the degradation pathways of L-cysteine and L-serine, and removing the repressor responsible for sulfur metabolism. Finally, the simultaneously introduction of gshF and enhancement of cysteine formation enabled C. glutamicum strain to produce glutathione greatly. Without external addition of L-cysteine and L-glutamate, 756mg/L glutathione was produced. This is first time to demonstrate the potential of the glutathione non-producing strain C. glutamicum for glutathione production and provide a novel strategy to construct glutathione-producing strains.

Structural and Chemical Evolution of l-Cysteine Nanofilm on Si(111)-√3×√3-Ag: From Preferential Growth at Step Edges and Antiphase Boundaries at Room Temperature to Adsorbate-Mediated Metal Cluster Formation at Elevated Temperature.

The interaction of cysteine molecules with the Si(111)-√3×√3-Ag surface has been investigated over the submonolayer to multilayer regime using X-ray photoelectron spectroscopy, scanning tunneling microscopy, and density functional theory calculations. With both upper step and lower step terraces, step edges, and antiphase boundaries, the √3×√3-Ag overlayer supported on Si(111) provides a rich two-dimensional template for studying site-specific biomolecular interactions. As an amino acid with three functional groups, cysteine is found to chemisorb through S-H bond cleavage and S-Ag bond linkage first at step edges and antiphase boundaries followed by island formation and expanded growth onto terraces. Intermolecular interactions are dominated by zwitterionic hydrogen bonding at higher coverages, producing a porous unordered interfacial layer composed of cysteine agglomerates at room temperature. Upon annealing, cysteine adsorbates induce structural transformation of the uniform √3×√3-Ag reconstructed surface lattice into metallic Ag clusters with a narrow size distribution and short-range ordering. Preferential nanoaggregate formation of cysteine at defect sites and cysteine-induced metal cluster formation promise a new approach to fabricating nanoclusters for potential applications in chemical sensing and catalysis.

P6003Coronary artery spasm: a consequence of impaired nitric oxide/hydrogen sulphide signalling?

Abstract Background Coronary artery spasm (CAS) represents a major cause of patient morbidity, with variable clinical response to prophylaxis with calcium antagonists and generally poor symptomatic relief with organic nitrates. The precipitation of CAS with acetylcholine may reflect impaired nitric oxide (NO) release and/or signalling. We have recently demonstrated that platelets from patients with CAS exhibit markedly impaired anti-aggregatory responses to the NO donor sodium nitroprusside (SNP) (“NO resistance”). Purpose In the current experiments we sought to determine whether N-acetylcysteine (NAC), which is known to potentiate haemodynamic responses to organic nitrates, reverses NO resistance in platelets from CAS patients. Methods Patients with CAS were studied during acute (n=11) and chronic (n=24) phases of symptoms. NAC (10 g/24 hours) was infused together with low dose NTG (2.5 μg/min) in patients presenting with acute exacerbations, and platelets were studied ex vivo. In blood samples taken from chronic CAS patients, in vitro studies were performed to evaluate the possible role of H2S release (via cysteine formation) from NAC in putative potentiation of NO effect. Results (1) In acute patients, NTG/NAC infusion resulted in increases in platelet response to SNP (p=0.003); (2) In vitro studies showed that incubation with NAC or the H2S donor NaHS potentiated SNP responses (Figure 1A); (3) Effects of NAC were reversed by co-incubation with aminooxyacetic acid (AOAA) and D, L-propargylglycine (PAG), inhibitors of enzymatic cysteine bioconversion to release H2S (Figure 1B). Figure 1 Conclusion CAS-associated impairment of platelet NO signaling reflects a deficiency of the H2S/NO interaction, and can be reversed using exogenous H2S donors, including NAC.

Turn-on fluorescence detection of cysteine with glutathione protected silver nanoclusters

In this work, we report a sensitive and selective turn-on fluorescence detection of cysteine with glutathione protected silver nanoclusters (GSH-Ag NCs). The glutathione stabilized silver nanoclusters were synthesized by the boiling water method. When excited at 380 nm, the GSH-Ag NCs exhibited a weak emission at about 680 nm, which could be enhanced by cysteine. The proposed method allows evaluation of cysteine in the range of 2–3000 μM with a detection limit of 0.51 μM. The recoveries were found to be 95.07%-101.38% when detecting cysteine contents in fetal bovine serum samples. In addition, we also discussed the possible mechanism for the fluorescence enhancement of GSH-Ag NCs by addition of cysteine. It might be the formation of cysteine and glutathione co-capped Ag NCs. This work reported a fluorimetric method for the assay of cysteine and provided a strategy for the synthesis of dual ligand-protected Ag nanoclusters.

Leiomyoma with bizarre nuclei: a morphological, immunohistochemical and molecular analysis of 31 cases

Leiomyomas associated with hereditary leiomyomatosis and renal cell carcinoma syndrome and leiomyomas with bizarre nuclei often show overlapping morphological features, in particular cells with prominent eosinophilic nucleoli, perinucleolar halos, and eosinophilic cytoplasmic inclusions. Although hereditary leiomyomatosis and renal cell carcinoma syndrome is defined by fumarate hydratase (FH) germline mutations, resulting in S-(2-succino)-cysteine (2SC) formation, it is unknown whether leiomyomas with bizarre nuclei show similar alterations. In this study, we evaluated the morphology and FH/2SC immunoprofile of 31 leiomyomas with bizarre nuclei. DNA from tumor and normal tissues from 24 cases was subjected to massively parallel sequencing targeting 410 key cancer genes. Somatic genetic alterations were detected using state-of-the-art bioinformatics algorithms. No patient reported a personal history of renal neoplasia or cutaneous leiomyomas, but one had a family history of renal cell carcinoma while another had a family history of uterine leiomyomas. Aberrant FH/2SC expression was noted in 17 tumors (16 FH-negative/2SC-positive, 1 FH-positive/2SC-positive). On univariate analysis, staghorn vessels, eosinophilic cytoplasmic inclusions, diffuse distribution of prominent eosinophilic nucleoli with perinucleolar halos, and an ‘alveolar pattern of edema’ were associated with an abnormal immunoprofile, but only staghorn vessels remained significant on multivariate analysis. Massively parallel sequencing analysis (n=24) revealed that 13/14 tumors with aberrant FH/2SC immunoprofile harbored somatic FH somatic genetic alterations, including homozygous deletions (n=9), missense mutations coupled with loss of heterozygosity (n=3), and a splice site mutation (n=1), whereas no somatic FH mutations/deletions were found in tumors with normal immunoprofile (n=10; P<0.0001). Leiomyomas with bizarre nuclei with normal FH/2SC staining pattern more frequently harbored TP53 and/or RB1 alterations than those with aberrant FH/2SC immunoprofile (60 vs 14%; P=0.032). These data demonstrate that leiomyomas with bizarre nuclei are morphologically and genetically heterogeneous and that hereditary leiomyomatosis and renal cell carcinoma syndrome-related morphological features, abnormal FH/2SC staining, and somatic FH mutations/deletions can be seen in a subset of sporadic tumors.

Facile electrosynthesis and characterization of superparamagnetic nanoparticles coated with cysteine, glycine and glutamine

A novel and facile strategy has been developed for the preparation of cysteine-, glycine- and glutamine-coated magnetite nanoparticles (MNPs). According to this strategy, Fe3O4 nanoparticles were electrodeposited from an aqueous electrolyte containing a dissolved iron salt and amino acids. A simple deposition mode i.e., constant current and two-electrode set-up was used in the electrosynthesis procedure. The magnetite phase of the deposited nanoparticles was confirmed through XRD and FT-IR analyses. Morphological observations through FE-SEM and TEM confirmed the formation of spherical MNP particles with an average size of 10 nm. The formation of cysteine, glycine and glutamine layers on the surface of the electro-synthesized particles was proved based on FT-IR, DLS and TG data. Vibrating sample magnetometery (VSM) measurements confirmed the prepared iron oxide nanoparticles to have a super-paramagnetic nature, since they exhibit a high saturation magnetization (Ms ≈ 58 emu g−1), as well as, negligible remnant magnetization (Mr) and coercivity (Ce). Based on the obtained results, the proposed platform can be considered as a fast, simple and efficient method for the preparation of surface-coated magnetite nanoparticles.

Dynamic genome-scale metabolic modeling of the yeast Pichia pastoris

BackgroundPichia pastoris shows physiological advantages in producing recombinant proteins, compared to other commonly used cell factories. This yeast is mostly grown in dynamic cultivation systems, where the cell’s environment is continuously changing and many variables influence process productivity. In this context, a model capable of explaining and predicting cell behavior for the rational design of bioprocesses is highly desirable. Currently, there are five genome-scale metabolic reconstructions of P. pastoris which have been used to predict extracellular cell behavior in stationary conditions.ResultsIn this work, we assembled a dynamic genome-scale metabolic model for glucose-limited, aerobic cultivations of Pichia pastoris. Starting from an initial model structure for batch and fed-batch cultures, we performed pre/post regression diagnostics to ensure that model parameters were identifiable, significant and sensitive. Once identified, the non-relevant ones were iteratively fixed until a priori robust modeling structures were found for each type of cultivation. Next, the robustness of these reduced structures was confirmed by calibrating the model with new datasets, where no sensitivity, identifiability or significance problems appeared in their parameters. Afterwards, the model was validated for the prediction of batch and fed-batch dynamics in the studied conditions.Lastly, the model was employed as a case study to analyze the metabolic flux distribution of a fed-batch culture and to unravel genetic and process engineering strategies to improve the production of recombinant Human Serum Albumin (HSA). Simulation of single knock-outs indicated that deviation of carbon towards cysteine and tryptophan formation improves HSA production. The deletion of methylene tetrahydrofolate dehydrogenase could increase the HSA volumetric productivity by 630%. Moreover, given specific bioprocess limitations and strain characteristics, the model suggests that implementation of a decreasing specific growth rate during the feed phase of a fed-batch culture results in a 25% increase of the volumetric productivity of the protein.ConclusionIn this work, we formulated a dynamic genome scale metabolic model of Pichia pastoris that yields realistic metabolic flux distributions throughout dynamic cultivations. The model can be calibrated with experimental data to rationally propose genetic and process engineering strategies to improve the performance of a P. pastoris strain of interest.

Enzyme Catalysis that Paves the Way for S-Sulfhydration via Sulfur Atom Transfer.

S-sulfhydration is generally anticipated to proceed through the transfer of the SH group (Nu-SH···(-)S-R → Nu(-)···HS-S-R). The other route involves the sulfur atom (S(0)) transfer between two sulfhydryl anions (Nu-S(-)···(-)S-R → Nu(-)···(-)S-S-R) and is considered electrostatically unfavorable. Mercaptopyruvate sulfurtransferase (MST, PDB code: 4JGT ) catalyzes sulfur transfer from mercaptopyruvate to sulfur acceptors, and the first step of the reaction is the formation of cysteine (Cys248) persulfide via S-sulfhydration. Mechanistic studies on S-sulfhydration in MST using QM/MM methods show that the sulfur atom transfer initialized by the deprotonation of the Ser250/His74/Asp63 triad is kinetically preferred to the SH-promoted sulfur transfer. The calculated barrier of approximately 16 kcal mol(-1) for the S(0) transfer agrees well with experimental results. The electrostatic repulsion during the S(0) transfer can be sophisticatedly reduced by the aid of the Cys248-Gly249-Ser250-Gly251-Val252-Thr253 (CGSGVT) loop. Electrostatic potentials and frontier orbitals are also analyzed for the persulfide anion surrounded by the loop. The sulfur atom transfer which is seldom regarded possible is therefore facilitated with the assistance of the triad and the loop in the enzyme.

Highly sensitive and selective detection of trinitrotoluene using cysteine-capped gold nanoparticles

(A) A schematic representation of the formation of cysteine capped gold nanoparticles and their interaction at pH 5 and 9.3. (B) A schematic representation of the formation of a Meisenheimer complex between cysteine modified gold nanoparticles and TNT, and possible cross-linking between gold nanoparticles bound to the Meisenheimer complex with gold nanoparticle bound cysteine.

An O-acetylserine (thiol) lyase from Leucaena leucocephala is a cysteine synthase but not a mimosine synthase.

In plants, the final step of cysteine formation is catalyzed by O-acetylserine (thiol) lyase (OAS-TL). The purpose of this study was to isolate and characterize an OAS-TL from the tree legume Leucaena leucocephala (leucaena). Leucaena contains a toxic, nonprotein amino acid, mimosine, which is also formed by an OAS-TL, and characterization of this enzyme is essential for developing a mimosine-free leucaena for its use as a protein-rich fodder. The cDNA for a cytosolic leucaena OAS-TL isoform was obtained through interspecies suppression subtractive hybridization. A 40-kDa recombinant protein was purified from Escherichia coli and used in enzyme activity assays where it was found to synthesize only cysteine. The enzyme followed Michaelis-Menten kinetics, and the Km was calculated to be 1,850±414 μM sulfide and the Vmax was 200.6±19.92 μM cysteine min(-1). The N-terminal affinity His-tag was cleaved from the recombinant OAS-TL to eliminate its possible interference in binding with the substrate, 3-hydroxy-4-pyridone, for mimosine formation. The His-tag-cleaved OAS-TL was again observed to catalyze the formation of cysteine but not mimosine. Thus, the cytosolic OAS-TL from leucaena used in this study is specific for only cysteine synthesis and is different from previously reported OAS-TLs that also function as β-substituted alanine synthases.

Comprehensive Cell-specific Protein Analysis in Early and Late Pollen Development from Diploid Microsporocytes to Pollen Tube Growth

Pollen development in angiosperms is one of the most important processes controlling plant reproduction and thus productivity. At the same time, pollen development is highly sensitive to environmental fluctuations, including temperature, drought, and nutrition. Therefore, pollen biology is a major focus in applied studies and breeding approaches for improving plant productivity in a globally changing climate. The most accessible developmental stages of pollen are the mature pollen and the pollen tubes, and these are thus most frequently analyzed. To reveal a complete quantitative proteome map, we additionally addressed the very early stages, analyzing eight stages of tobacco pollen development: diploid microsporocytes, meiosis, tetrads, microspores, polarized microspores, bipolar pollen, desiccated pollen, and pollen tubes. A protocol for the isolation of the early stages was established. Proteins were extracted and analyzed by means of a new gel LC-MS fractionation protocol. In total, 3817 protein groups were identified. Quantitative analysis was performed based on peptide count. Exceedingly stage-specific differential protein regulation was observed during the conversion from the sporophytic to the gametophytic proteome. A map of highly specialized functionality for the different stages could be revealed from the metabolic activity and pronounced differentiation of proteasomal and ribosomal protein complex composition up to protective mechanisms such as high levels of heat shock proteins in the very early stages of development.

Application of the Generalized Connectivity-Based Hierarchy to Biomonomers: Enthalpies of Formation of Cysteine and Methionine

Computational challenges toward an accurate determination of the enthalpies of formation of amino acids are partly due to the nonavailability of systematic error-canceling thermochemical procedures for such biomonomers. Recently, we developed the connectivity-based hierarchy (CBH) to accurately compute the enthalpies of formations of organic molecules composed of main group elements. Advancing the applicability of CBH to biologically relevant molecules, we have computed the enthalpies of formation of the naturally occurring sulfur-containing amino acids cysteine and methionine which act as fertile testing grounds for the error-canceling ability of thermochemical schemes for biomolecules. We establish herein using the sophisticated error-canceling isoatomic scheme (CBH-2) that relatively inexpensive computational methods with modest basis sets can be used to accurately obtain the enthalpies of formations of the amino acids. Overall, we recommend the use of the isoatomic scheme over the currently popular isodesmic bond separation scheme in future applications in theoretical thermochemistry.

Characterization of O‐acetylserine (thiol) lyase from Leucaena leucocephala

In plants, the final step of cysteine formation involves the addition of sulfide to O‐acetylserine (OAS) and the release of acetate, catlyzed by O‐acetylserine (thiol) lyase (OASTL). The purpose of this study was to isolate and characterize recombinant OASTL from Leucaena leucocephala (leucaena), a protein‐rich legume used as a fodder. Leucaena contains a toxic, nonprotein amino acid, mimosine, which is also produced by OASTL. In order to understand the function of this enzyme, we first studied cysteine synthesis. The cDNA for a cytosolic OASTL was obtained through interspecies subtractive hybridization and Rapid Amplification of cDNA Ends. The sequence was codon optimized and expressed in Escherichia coli under the control of a T7 promoter. A 37‐kDa protein was isolated and used in in vitro enzyme activity assays with Na2S and OAS as substrates where cysteine was detected and quantified using High Performance Liquid Chromatography. The Km was 1.850±0.4146 mM Na2S and the Vmax was 200.6±19.92 μM cysteine minute−1. Central to the mimosine and cysteine biosynthetic pathways is OASTL. Characterization of this enzyme will be essential in the development of a toxin‐free leucaena for its use as a widespread forage crop. This research was funded by NSF Award No. CBET 08–27057.

Assessing functional diversity in the soybean β-substituted alanine synthase enzyme family

In plants, proteins of the β-substituted alanine synthase (BSAS) enzyme family perform a diverse range of reactions, including formation of cysteine from O-acetylserine and sulfide, detoxification of cyanide by its addition to cysteine, the breakdown of cysteine into pyruvate, ammonia, and sulfide, and the synthesis of S-sulfocysteine. With the completed genome sequence of soybean (Glycine max (L.) Merr. cv. Williams 82), the functional diversity of the BSAS in this highly duplicated plant species was examined to determine whether soybean BSAS enzymes catalyze the various reactions connected to cysteine metabolism. The 16 soybean BSAS can be grouped into clades that are similar to those observed in Arabidopsis. Biochemical analysis of soybean BSAS proteins demonstrate that enzymes of clades I and III function as O-acetylserine sulfhydrylases for cysteine synthesis, clade II encodes cysteine desulfhydrase activity, and that clade V proteins function as β-cyanoalanine synthase for cyanide detoxification. Although clade IV is similar to Arabidopsis S-sulfocysteine synthase, this activity was not detected in the soybean homolog. Overall, our results show that bioinformatics approach provides a useful method to assess the biochemical properties of BSAS enzymes in plant species.

Cysteine formation with Corynebacterium glutamicum and intracellular sensing of O-acetylserine

Cysteine formation with Corynebacterium glutamicum and intracellular sensing of O-acetylserine