| [mode of action of d-amino acids on the biosynthesis of peptidoglycan (author's transl)]. | the mechanism of growth inhibition by d-amino acids was studied. d-serine at concentrations from 0.02-0.2 m was sufficient to cause partial growth inhibition in seven species of bacteria representing the four most common types of peptidoglycan. the inhibited cells displayed morphological alterations. in the nucleotide-activated peptidoglycan precursors of these cells, d-alanine residues in position 4 and/or 5 of the peptide moiety were partially or even completely replaced by d-serine. the pepti ... | 1976 | 825075 |
| some properties of glutamate dehydrogenase, glutamine synthetase and glutamate synthase from corynebacterium callunae. | characteristics of the three major ammonia assimilatory enzymes, glutamate dehydrogenase (gdh), glutamine synthetase (gs) and glutamate synthase (go-gat) in corynebacterium callunae (ncib 10338) were examined. the gdh of c. callunae specifically required nadph and nadp+ as coenzymes in the amination and deamination reactions, respectively. this enzyme showed a marked specificity for alpha-ketoglutarate and glutamate as substrates. the optimum ph was 7.2 for nadph-gdh activity (amination) and 9.0 ... | 1992 | 1359847 |
| the effect of various culture conditions on the levels of ammonia assimilatory enzymes of corynebacterium callunae. | corynebacterium callunae (ncib 10338) grows faster on glutamate than ammonia when used as sole nitrogen sources. the levels of glutamine synthetase (gs; ec 6.3.1.2) and glutamate synthase (gogat; ec 1.4.1.13) of c. callunae were found to be influenced by the nitrogen source. accordingly, the levels of gs and gogat activities were decreased markedly under conditions of ammonia excess and increased under low nitrogen conditions. in contrast, glutamate dehydrogenase (gdh; ec 1.4.1.4) activities wer ... | 1992 | 1359848 |
| transfer of brevibacterium divaricatum dsm 20297t, "brevibacterium flavum" dsm 20411, "brevibacterium lactofermentum" dsm 20412 and dsm 1412, and corynebacterium glutamicum and their distinction by rrna gene restriction patterns. | the results of dna-dna hybridization and chemotaxonomic studies indicated that the glutamic acid producers brevibacterium divaricatum dsm 20297t (t=type strain), "brevibacterium flavum" dsm 20411, "brevibacterium lactofermentum" dsm 1412 and dsm 20412, corynebacterium lilium dsm 20137t, and corynebacterium glutamicum dsm 20300t and dsm 20163 are members of the same species. it is proposed that all of these strains should be classified in the species corynebacterium glutamicum. another glutamic a ... | 1991 | 1713055 |
| alpha-1,4-d-glucan phosphorylase of gram-positive corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution x-ray scattering. | the alpha-1,4-d-glucan phosphorylase from gram-positive corynebacterium callunae has been isolated and characterized. the enzyme is inducible approx. 2-fold by maltose, but remarkably not repressed by d-glucose. the phosphorylase is a homodimer with a stoichiometric content of the cofactor pyridoxal 5'-phosphate per 88-kda protein subunit. the specificity constants (kcat/km, glucan) in the directions of glucan synthesis and degradation are used for the classification of the enzyme as the first b ... | 1997 | 9307027 |
| thermal denaturation pathway of starch phosphorylase from corynebacterium callunae: oxyanion binding provides the glue that efficiently stabilizes the dimer structure of the protein. | starch phosphorylase from corynebacterium callunae is a dimeric protein in which each mol of 90 kda subunit contains 1 mol pyridoxal 5'-phosphate as an active-site cofactor. to determine the mechanism by which phosphate or sulfate ions bring about a greater than 500-fold stabilization against irreversible inactivation at elevated temperatures (> or = 50 degrees c), enzyme/oxyanion interactions and their role during thermal denaturation of phosphorylase have been studied. by binding to a protein ... | 2000 | 10892808 |
| corynebacterium efficiens sp. nov., a glutamic-acid-producing species from soil and vegetables. | three glutamic-acid-producing coryneform strains were isolated from soil and vegetable samples. chemotaxonomic investigations indicated that these strains belonged to the genus corynebacterium. phylogenetic studies, based on 16s rdna analysis, demonstrated that the three strains formed a distinct cluster within the genus corynebacterium and that their nearest relatives were corynebacterium glutamicum and corynebacterium callunae, also known as glutamic-acid-producing species. the data from 16s r ... | 2002 | 12148616 |
| tracking interactions that stabilize the dimer structure of starch phosphorylase from corynebacterium callunae. roles of arg234 and arg242 revealed by sequence analysis and site-directed mutagenesis. | glycogen phosphorylases (gps) constitute a family of widely spread catabolic alpha1,4-glucosyltransferases that are active as dimers of two identical, pyridoxal 5'-phosphate-containing subunits. in gp from corynebacterium callunae, physiological concentrations of phosphate are required to inhibit dissociation of protomers and cause a 100-fold increase in kinetic stability of the functional quarternary structure. to examine interactions involved in this large stabilization, we have cloned and seq ... | 2003 | 12752432 |
| mutagenesis of the dimer interface region of corynebacterium callunae starch phosphorylase perturbs the phosphate-dependent conformational relay that enhances oligomeric stability of the enzyme. | we have used alanine-scanning site-directed mutagenesis of the dimer contact region of starch phosphorylase from corynebacterium callunae to explore the relationship between a protein conformational change induced by phosphate binding and the up to 500-fold kinetic stabilization of the functional quarternary structure of this enzyme when phosphate is present. purified mutants (at positions ser-224, arg-226, arg-234, and arg-242) were characterized by fourier transform-infrared (ft-ir) spectrosco ... | 2003 | 14607988 |
| characterization of the cryptic plasmid pcc1 from corynebacterium callunae and its use for vector construction. | the complete nucleotide sequence of the cryptic plasmid pcc1 from corynebacterium callunae (4109 bp) was determined. dna sequence analysis revealed five open reading frames longer than 200 bp. one of the deduced polypeptides showed homology with the rep proteins encoded by plasmids of the pij101/pjv1 family of plasmids replicating by the rolling-circle (rc) mechanism. within this plasmid family, the rep protein of pcc1 showed the highest degree of similarity to the rep proteins of corynebacteria ... | 2004 | 14711530 |
| relationships between structure, function and stability for pyridoxal 5'-phosphate-dependent starch phosphorylase from corynebacterium callunae as revealed by reversible cofactor dissociation studies. | using 0.4 m imidazole citrate buffer (ph 7.5) containing 0.1 mm l-cysteine, homodimeric starch phosphorylase from corynebacterium calluane (ccstp) was dissociated into native-like folded subunits concomitant with release of pyridoxal 5'-phosphate and loss of activity. the inactivation rate of ccstp under resolution conditions at 30 degrees c was, respectively, four- and threefold reduced in two mutants, arg234-->ala and arg242-->ala, previously shown to cause thermostabilization of ccstp [griess ... | 2004 | 15291809 |
| catalytic mechanism of alpha-retaining glucosyl transfer by corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants. | purified site-directed mutants of corynebacterium callunae starch phosphorylase in which his-334 was replaced by an alanine, glutamine or asparagine residue were characterized by steady-state kinetic analysis of enzymic glycosyl transfer to and from phosphate and studies of ligand binding to the active site. compared with wild-type, the catalytic efficiencies for phosphorolysis of starch at 30 degrees c and ph 7.0 decreased approx. 150- and 50-fold in h334q (his334-->gln) and h334n mutants, and ... | 2005 | 15535798 |
| porh, a new channel-forming protein present in the cell wall of corynebacterium efficiens and corynebacterium callunae. | corynebacterium callunae and corynebacterium efficiens are close relatives of the glutamate-producing mycolata species corynebacterium glutamicum. the properties of the pore-forming proteins, extracted by organic solvents, were studied. the cell extracts contained channel-forming proteins that formed ion-permeable channels with a single-channel conductance of about 2 to 3 ns in 1 m kcl in a lipid bilayer assay. the corresponding proteins from both corynebacteria were purified to homogeneity and ... | 2005 | 16000733 |
| probing the active site of corynebacterium callunae starch phosphorylase through the characterization of wild-type and his334-->gly mutant enzymes. | his334 facilitates catalysis by corynebacterium callunae starch phosphorylase through selective stabilization of the transition state of the reaction, partly derived from a hydrogen bond between its side chain and the c-6 hydroxy group of the glucosyl residue undergoing transfer to and from phosphate. we have substituted his334 by a gly and measured the disruptive effects of the site-directed replacement on active site function using steady-state kinetics and nmr spectroscopic characterization o ... | 2007 | 17803683 |
| studying non-covalent enzyme carbohydrate interactions by std nmr. | saturation transfer difference nmr spectroscopy is used to study non-covalent interactions between four different glycostructure transforming enzymes and selected substrates and products. resulting binding patterns represent a molecular basis of specific binding between ligands and biocatalysts. substrate and product binding to aspergillus fumigatus glycosidase and to candida tenuis xylose reductase are determined under binding-only conditions. measurement of std effects in substrates and produc ... | 2008 | 18281024 |
| reaction engineering aspects of alpha-l,4-d-glucan phosphorylase catalysis : comparison of plant and bacterial enzymes for the continuous synthesis of d-glucose-1-phosphate. | some important process properties of alpha-l,4-d-glucan phosphorylases isolated from the bacterium corynebacterium callunae and potato tubers (solatium tuberosum) were compared. apart from minor differences in their stability and specificity (represented by the maximum degree of maltodextrin conversion) and a 10-fold higher affinity of the plant phosphorylase for maltodextrin (k (m) of 1.3 g/l at 300 mm of orthophosphate), the performances of both enzymes in a continuous ultrafiltration membrane ... | 1997 | 18576079 |
| characterization of developmental colony formation in corynebacterium glutamicum. | we report that corynebacterium glutamicum colonies exhibit a developmental transition in culture. when cultured on a routinely used complete medium (cm2b), this bacterium first formed a flat translucent colony. subsequently, some parts of this colony expanded to form small spherical yellow colonies that finally developed into a single large yellow colony. the small flat colony consisted of long thick cells, which were occasionally v or y shaped, while the large yellow colony consisted of short s ... | 2008 | 18696061 |
| reconstitution experiments and gene deletions reveal the existence of two-component major cell wall channels in the genus corynebacterium. | two small polypeptides, pora and porh, are known to form cell wall channels in corynebacterium glutamicum and in corynebacterium efficiens. the genes coding for both polypeptides are localized in close proximity to one another between the genes coding for groel2 and a polyphosphate kinase (pkk2). in this study, we investigated the relationship of pora and porh to one another. the results suggested that the major cell wall channels of corynebacterium glutamicum, corynebacterium efficiens, and cor ... | 2010 | 19966008 |
| orthophosphate binding at the dimer interface of corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme. | orthophosphate recognition at allosteric binding sites is a key feature for the regulation of enzyme activity in mammalian glycogen phosphorylases. protein residues co-ordinating orthophosphate in three binding sites distributed across the dimer interface of a non-regulated bacterial starch phosphorylase (from corynebacterium callunae) were individually replaced by ala to interrogate their unknown function for activity and stability of this enzyme. | 2010 | 20113461 |
| microbial diversity and dynamics during the production of may bryndza cheese. | diversity and dynamics of microbial cultures were studied during the production of may bryndza cheese, a traditional slovak cheese produced from unpasteurized ewes' milk. quantitative culture-based data were obtained for lactobacilli, lactococci, total mesophilic aerobic counts, coliforms, e. coli, staphylococci, coagulase-positive staphylococci, yeasts, fungi and geotrichum spp. in ewes' milk, curd produced from it and ripened for 0 - 10 days, and in bryndza cheese produced from the curd, in th ... | 2014 | 24291178 |
| production of para-aminobenzoate by genetically engineered corynebacterium glutamicum and non-biological formation of an n-glucosyl byproduct. | para-aminobenzoate (paba), a valuable chemical raw material, can be synthesized by most microorganisms. this aromatic compound is currently manufactured from petroleum-derived materials by chemical synthesis. to produce paba from renewable resources, its production by fermentation was investigated. the evaluation of the sensitivity to paba toxicity revealed that corynebacterium glutamicum had better tolerance to paba than several other microorganisms. to produce paba from glucose, genetically en ... | 2016 | 27471069 |
| corynebacterium crudilactis sp. nov., isolated from raw cow's milk. | a gram-stain-positive, rod-shaped bacterium (strain jz16t) was isolated from raw cow's milk from the bulk tank of a dairy farm in germany. the 16s rrna gene sequence of the isolate showed a similarity of 98.3 % to the nearest related type strain corynebacterium glutamicum atcc 13032t, a similarity of 97.6 % to corynebacterium deserti gimn1.010t and a similarity of 97.4 % to corynebacterium callunae dsm 20147t. determination of chemotaxonomic characteristics revealed oleic acid (18 : 1 cis 9) as ... | 2016 | 27666312 |
| corynebacterium defluvii sp. nov., isolated from sewage. | a gram-positive, aerobic, non-motile, rod-shapeds, catalase-positive, and oxidase-negative strain, designated y49(t), was isolated from sewage collected from jilin agricultural university, china. it grew at 20-40°c (optimum at 30°c), at ph 6.0-8.0 (optimum at 7.0) and at 0-1.0% sodium chloride (optimum at 0%). the major isoprenoid quinone was menaquinone-8 (mk-8) and the polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylmethylethanolamine, four unidentified lipids, and ... | 0 | 28429167 |
| complete genome sequencing of newly isolated thermotolerant corynebacterium glutamicum n24 provides a new insights into its thermotolerant phenotype. | to understand the genetic background of thermotolerance, we determined the complete genome sequence of a thermotolerant corynebacterium glutamicum n24 strain isolated from soil. the whole genome based phylogenetic analysis between n24 and other related species revealed that n24 diverged from other c. glutamicum strains at earlier stages. comparisons of thermotolerance between n24 and its related species showed that n24 and corynebacterium efficiens ys-314 have a higher thermotolerance than coryn ... | 2017 | 28249784 |
| genome sequence of the soil bacterium corynebacterium callunae type strain dsm 20147(t). | corynebacterium callunae dsm 20147(t) is a member of the genus corynebacterium which contains gram-positive and non-spore forming bacteria with a high g + c content. c. callunae was isolated during a screening for l-glutamic acid producing bacteria and belongs to the aerobic and non-haemolytic corynebacteria. as this is a type strain in a subgroup of industrial relevant bacteria for many of which there are also complete genome sequence available, knowledge of the complete genome sequence might e ... | 2015 | 26203323 |