A naturally deficient thiamine and methionine requiring strain of Bacillus coagulans (Ms 5) accumulates lysine in medium only when exogenous pyridoxine (optimal concentration, 0.1 mu g/ml) are supplied. Threonine exerts an inhibitory effect at higher concentrations but pyridoxine does not.

• MeSH
• Bacillus classification   growth & development   metabolism   MeSH
• Colorimetry MeSH
• Lysine biosynthesis   MeSH
• Methionine metabolism   MeSH
• Mutation * MeSH
• Chromatography, Paper MeSH
• Pyridoxine metabolism   MeSH
• Thiamine metabolism   MeSH
• Threonine metabolism   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Lysine MeSH
• Methionine MeSH
• Pyridoxine MeSH
• Thiamine MeSH
• Threonine MeSH

• Keywords
• BIOLOGICAL ASSAY *, ESCHERICHIA COLI *, EXPERIMENTAL LAB STUDY *, LYSINE *,
• MeSH
• Biological Assay * MeSH
• Escherichia coli * MeSH
• Lysine * MeSH
• Research * MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Lysine * MeSH

The widespread occurrence of cyanobacteria blooms damages the water ecosystem and threatens the safety of potable water and human health. Exogenous L-lysine significantly inhibits the growth of a dominant cyanobacteria Microcystis aeruginosa in freshwater. However, the molecular mechanism of how lysine inhibits the growth of M. aeruginosa is unclear. In this study, both non-target and target metabolomic analysis were performed to investigate the effects of algicide L-lysine. The results showed that 8 mg L- 1 lysine most likely disrupts the metabolism of amino acids, especially the arginine and proline metabolism. According to targeted amino acid metabolomics analysis, only 3 amino acids (L-arginine, ornithine, and citrulline), which belong to the ornithine-ammonia cycle (OAC) in arginine metabolic pathway, showed elevated levels. The intracellular concentrations of ornithine, citrulline, and arginine increased by 115%, 124%, and 19.4%, respectively. These results indicate that L-lysine may affect arginine metabolism and OAC to inhibit the growth of M. aeruginosa.

• Keywords
• Arginine metabolism, L-lysine, Metabolomic analysis, Microcystin, Microcystis aeruginosa, Ornithine-ammonia cycle,
• MeSH
• Ammonia MeSH
• Arginine chemistry   metabolism   MeSH
• Citrulline metabolism   MeSH
• Ecosystem MeSH
• Herbicides * metabolism   MeSH
• Humans MeSH
• Lysine toxicity   metabolism   MeSH
• Microcystis * metabolism   MeSH
• Microcystins metabolism   MeSH
• Ornithine toxicity   metabolism   MeSH
• Cyanobacteria * metabolism   MeSH
• Check Tag
• Humans MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Ammonia MeSH
• Arginine MeSH
• Citrulline MeSH
• Herbicides * MeSH
• Lysine MeSH
• Microcystins MeSH
• Ornithine MeSH

A kinetic approach is proposed to shorten the microbiological assay time for the determination of unbound L-lysine. The present lysine bacterial assay takes from 16 to 24 h using Pediococcus cerevisiae P-60 ATCC 8042 (formerly Leuconostoc mesenteroides P-60 ATCC 8042) and uses a medium in which lysine is the limiting substance. Measurements of the final cell concentration are linearly correlated with the initial concentration of lysine, S, to provide an indirect estimate of S. We propose to understand the limitations inherent to the reduction of the assay time to 4 h by focusing in our analysis on the bacterial late lag or early growth transient phases, rather than the stationary phase of growth. Generally, the Monod equation is expected to describe a hyperbolically increasing correlation between the bacterial specific growth rate at about 2-4 h and the initial lysine concentration. A hyperbolic correlation is obtained by 3 h, but the lysine region of interest falls in the saturated portion of the curve. Discriminations between different initial lysine levels are therefore difficult with this nearly flat curve. On the other hand, when the initial inoculum level is lowered, so that substrate inhibition becomes effective, a correlation with a large negative slope is obtained by 4 h. Limitations to using absorbance measurements for the rapid assay turn up in a lack of reproducibility and, hence, a large variance associated with the measurements. Alternative microbial measuring techniques, such as impedance methods, need to be examined in order to reduce that large variance.

• MeSH
• Models, Biological MeSH
• Biological Assay methods   MeSH
• Lysine analysis   metabolism   MeSH
• Pediococcus growth & development   metabolism   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Lysine MeSH

Post-translational modifications of proteins enable swift physiological adaptation of cells to altered growth conditions and stress. Aside from protein phosphorylation, acetylation on ε-amino groups of lysine residues (N-ε-lysine acetylation) represents another important post-translational modification of proteins. For many bacterial pathogens, including the whooping cough agent Bordetella pertussis, the role and extent of protein acetylation remain to be defined. We expressed in Escherichia coli the BP0960 and BP3063 genes encoding two putative deacetylases of B. pertussis and show that BP0960 encodes a lysine deacetylase enzyme, named Bkd1, that regulates acetylation of a range of B. pertussis proteins. Comparison of the proteome and acetylome of a Δbkd1 mutant with the proteome and acetylome of wild-type B. pertussis (PRIDE ID. PXD016384) revealed that acetylation on lysine residues may modulate activities or stabilities of proteins involved in bacterial metabolism and histone-like proteins. However, increased acetylation of the BvgA response regulator protein of the B. pertussis master virulence-regulating BvgAS two-component system affected neither the total levels of produced BvgA nor its phosphorylation status. Indeed, the Δbkd1 mutant was not impaired in the production of key virulence factors and its survival within human macrophages in vitro was not affected. The Δbkd1 mutant exhibited an increased growth rate under carbon source-limiting conditions and its virulence in the in vivo mouse lung infection model was somewhat affected. These results indicate that the lysine deacetylase Bkd1 and N-ε-lysine acetylation primarily modulate the general metabolism rather than the virulence of B. pertussis.

• Keywords
• Bkd1, Bordetella pertussis, KDAC, acetylome, deacetylation, post-translational modification,
• MeSH
• Acetylation MeSH
• Bacterial Proteins * genetics   metabolism   MeSH
• Bordetella pertussis genetics   MeSH
• Lysine * metabolism   MeSH
• Mice MeSH
• Gene Expression Regulation, Bacterial MeSH
• Virulence MeSH
• Animals MeSH
• Check Tag
• Mice MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Bacterial Proteins * MeSH
• Lysine * MeSH

To improve the yield of lysine by the isolate, auxotrophic mutants were isolated. Among the mutants, only one auxotrophic mutant required vitamin B12. This mutant produced alpha-alanine. About 200 mutants resistant to the lysine analog S-(2-aminoethyl)-L-cysteine were isolated and some of them produced well above the wild type.

• MeSH
• Alanine biosynthesis   MeSH
• Drug Resistance, Microbial genetics   MeSH
• Arthrobacter genetics   isolation & purification   metabolism   MeSH
• Bacteriological Techniques MeSH
• Cysteine analogs & derivatives   pharmacology   MeSH
• Lysine biosynthesis   MeSH
• Methylnitronitrosoguanidine MeSH
• Mutation MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Alanine MeSH
• Cysteine MeSH
• Lysine MeSH
• Methylnitronitrosoguanidine MeSH
• S-2-aminoethyl cysteine MeSH Browser

EHT and CNDO/2 types of calculations permit the interpretation of the course of hydroxylation of collagenous proline and lysine. Calculations were performed for the models of proline (I), zwitterion of proline (II), proline-containing peptide (III), and lysine (IV). The theoretical results are consistent with an electrophilic mechanism.

• MeSH
• Electrochemistry methods   MeSH
• Hydroxylation MeSH
• Hydroxylysine chemistry   MeSH
• Hydroxyproline chemistry   MeSH
• Collagen chemistry   MeSH
• Protein Conformation MeSH
• Lysine chemistry   MeSH
• Molecular Conformation MeSH
• Models, Molecular MeSH
• Proline chemistry   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Hydroxylysine MeSH
• Hydroxyproline MeSH
• Collagen MeSH
• Lysine MeSH
• Proline MeSH

In an effort to establish reliable thermodynamic data for amino acids, heat capacity and phase behavior are reported for L-cysteine (CAS RN: 52-90-4), L-serine (CAS RN: 56-45-1), L-threonine (CAS RN: 72-19-5), L-lysine (CAS RN: 56-87-1), and L-methionine (CAS RN: 63-68-3). Prior to heat capacity measurements, initial crystal structures were identified by X-ray powder diffraction, followed by a thorough investigation of the polymorphic behavior using differential scanning calorimetry in the temperature range from 183 K to the decomposition temperature determined by thermogravimetric analysis. Crystal heat capacities of all five amino acids were measured by Tian-Calvet calorimetry in the temperature interval (262-358) K and by power compensation DSC in the temperature interval from 215 K to over 420 K. Experimental values of this work were compared and combined with the literature data obtained with adiabatic calorimetry. Low-temperature heat capacities of L-threonine and L-lysine, for which no or limited literature data was available, were measured using the relaxation (heat pulse) calorimetry. As a result, reference heat capacities and thermodynamic functions for the crystalline phase from near 0 K to over 420 K were developed.

• Keywords
• L-cysteine, L-lysine, L-methionine, L-serine, L-threonine, crystalline phase, heat capacity,
• MeSH
• Cysteine chemistry   MeSH
• Lysine * MeSH
• Methionine MeSH
• Serine MeSH
• Threonine MeSH
• Hot Temperature * MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Cysteine MeSH
• Lysine * MeSH
• Methionine MeSH
• Serine MeSH
• Threonine MeSH

Systems of L-lysine transport in Schizosaccharomyces pombe are not constitutive, as at no phase of growth in a rich medium is lysine taken up. Transport activity appears only after preincubation of harvested cells with glucose or another suitable source of energy. If cycloheximide is added during this preincubation no transport systems are synthesized. After removal of glucose, the activity of the transport system decays with a half-time of 13 min. The transport of L-lysine into S. pombe cells from the stationary phase of growth preincubated for 60 min with 1% D-glucose is mediated by at least two systems, the high-affinity one with a Kt of 26 mumol/l and Jmax of 4.95 nmol/min per mg dry wt., the low-affinity one with a KT of 1.1 mmol/l and Jmax of 11.8 nmol/min per mg dry wt. The transport of lysine mediated by these two systems proceeds uphill. The high-affinity system has a pH optimum at 4.0-4.2, the accumulation ratio is highest at a cell density 2-5 mg dry wt. per ml and decreases with increasing lysine concentrations. Lysine accumulated by this system does not exit from cells. The only potent competitive inhibitors are L-arginine, L-histidine and D-lysine. The other amino acids tested do not behave as competitive inhibitors. Of the various metabolic inhibitors tested, the most potent were proton conductors and antimycin A.

• MeSH
• Biological Transport, Active MeSH
• Cycloheximide pharmacology   MeSH
• Hydrogen-Ion Concentration MeSH
• Lysine pharmacokinetics   MeSH
• Saccharomycetales metabolism   MeSH
• Schizosaccharomyces metabolism   MeSH
• Temperature MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Cycloheximide MeSH
• Lysine MeSH

A gap1 can1 mutant of Saccharomyces cerevisiae with a single lysine transport system remaining was used to study detailed kinetics of this transport. Its half-saturation constant was 78 mumol per litre, its maximum rate of transport was 0.29 mumol L-lysine per g dry matter per minute, both parameters being lower by more than an order of magnitude in comparison with the GAP system. The pH optimum lay at very acid values of about 3, the temperature dependence without any transition point showed an activation energy of 48 kJ/mol. The transport was inhibited by common metabolic inhibitors (3'-chlorophenylhydrazonomalononitrile, antimycin, 2-deoxy-D-glucose, sodium arsenate) as well as by a membrane-active one (uranyl nitrate). The specificity of the system was extremely high, none of the natural amino acids acting as competitor to L-lysine. The maximum accumulation ratio attained (at about 5 mg dry matter per mL) was 100: 1-120: 1, in agreement with the measured protonmotive force under the assumption of 1 H+ ion being transported with 1 lysine molecule. The ratio decreased with increasing external concentration of lysine to as little as 4: 1 at 1 mmol lysine per litre. It also decreased with increasing suspension density and it was at extremely low suspension densities (0.2 mg dry matter per mL) that ratios of as much as 500: 1 were reached. Application of group-specific inhibitors showed that the active site of the carrier contains an essential histidine residue.

• MeSH
• Glucose metabolism   MeSH
• Hydrogen-Ion Concentration MeSH
• Lysine pharmacokinetics   pharmacology   MeSH
• Saccharomyces cerevisiae drug effects   genetics   metabolism   MeSH
• Oxygen Consumption drug effects   MeSH
• Temperature MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Glucose MeSH
• Lysine MeSH