Bactofencin YH, a novel bacteriocin with high inhibitory activity against clinical Streptococcus species.

Strain Lactiplantibacillus plantarum D1 with bacteriocin producing ability was found in the intestine of Gambusia affinis. The bacteriocin was found to have high inhibitory activity against multiple Streptococcus species and several other Gram-positive and Gram-negative bacteria. Bacteriocin was purified from culture supernatant by ion-exchange chromatography, Sep-Pak C cartridge, and reverse-phase high-performance liquid chromatography (RP-HPLC).

Silica-associated proteins from hexactinellid sponges support an alternative evolutionary scenario for biomineralization in Porifera.

Metazoans use silicon traces but rarely develop extensive silica skeletons, except for the early-diverging lineage of sponges. The mechanisms underlying metazoan silicification remain incompletely understood, despite significant biotechnological and evolutionary implications. Here, the characterization of two proteins identified from hexactinellid sponge silica, hexaxilin and perisilin, supports that the three classes of siliceous sponges (Hexactinellida, Demospongiae, and Homoscleromorpha) use independent protein machineries to build their skeletons, which become non-homologous structures.

Acetylation of amines and alcohols catalyzed by acetylcholinesterase from Pseudomonas aeruginosa PAO1.

Acetylcholinesterase (AChE) from Pseudomonas aeruginosa PAO1 has a catalytic Ser residue in its active site. In this study, we examined the aminolysis and alcoholysis reactions of AChE that occurred alongside its hydrolysis reaction. The recombinant AChE recognized ethyl acetate as a substrate.

Production and characterization of cyanocobalamin-enriched tomato (Solanum lycopersicum) fruits grown using hydroponics.

Background: Vitamin B is an essential vitamin that is absent in plant-derived foods such as fruits and vegetables. This can result in an increased risk of developing vitamin B deficiency in strict vegetarians (vegans). There are several studies that have aimed to enhance nutrients in food crops.

Silica adsorption tag derived from the silica polycondensation protein glassin for the immobilization of soluble proteins.

Glassin is a water-soluble protein from the siliceous skeleton of a marine sponge that adsorbs tightly to silica at pH 7.0-9.0 and accelerates silica particle formation from silicic acid.

Chemicals behind the use of Strombus tricornis opercula in traditional sudanese perfumery and medicine.

Strombidae is one of the major molluscan families in Sudan and due to their opercula, has tremendous economic value. In traditional Sudanese homemade perfumes and body care cosmetics, Strombidae family operculum is one of the main ingredients. Their fumigation generates a charming odor preferred by Sudanese people, used for body smoke baths by married women.

Argeloside I inhibits the pathogenicity of Porphyromonas gingivalis TDC60.

Porphyromonas gingivalis, a major pathogen associated with chronic periodontitis, produces several virulence agents in the outer cell membrane, including gingipains and hemagglutinins. These virulence factors enable the bacteria to adhere to periodontal tissue and degrade host proteins to obtain the nutrients needed for dental plaque formation. P.

Chitinolytic proteins secreted by Cellulosimicrobium sp. NTK2.

Cellulosimicrobium sp. NTK2 (NTK2 strain) was isolated as a chitinolytic bacterium from mature compost derived from chitinous waste. The growth of the NTK2 strain was enhanced by supplementation of the culture medium with 2% crystalline chitin.

Involvement of Spermidine in the Reduced Lifespan of During Vitamin B Deficiency.

Vitamin B deficiency leads to various symptoms such as neuropathy, growth retardation, and infertility. Vitamin B functions as a coenzyme for two enzymes involved in amino acid metabolisms. However, there is limited information available on whether amino acid disorders caused by vitamin B deficiency induce such symptoms.

Isolates from Monechma ciliatum seeds' extract hampered Porphyromonas gingivalis hemagglutinins.

Porphyromonas gingivalis is a major periodontitis pathogen that produces several virulence factors including hemagglutinins. These proteins, which are vital molecules, allow P. gingivalis to uptake iron and heme by attaching, aggregating, and lysing erythrocytes.

Effect of Active Site Pocket Structure Modification of D-Stereospecific Amidohydrolase on the Recognition of Stereospecific and Hydrophobic Substrates.

D-Stereospecific amidohydrolase (DAH) from Streptomyces sp. 82F2 has potential utility for the synthesis of D/L configuration dipeptides by an aminolysis reaction. Structural comparison of DAH with substrate-bound D-amino acid amidase revealed that three residues located in the active site pocket of DAH (Thr145, Ala267, and Gly271) might be involved in interactions with D-phenylalanine substrate.

Active site pocket of Streptomycesd-stereospecific amidohydrolase has functional roles in aminolysis activity.

d-Stereospecific amidohydrolase from Streptomyces sp. 82F2 (DAH) recognizes d-amino acyl ester derivatives as substrates and catalyzes hydrolysis and aminolysis to yield d-amino acids and d-amino acyl peptides or amide derivatives, respectively. Crystallographic analysis has revealed that DAH possesses a large cavity with a small pocket at the bottom.

Methionine residues lining the substrate pathway in prolyl oligopeptidase from Pleurotus eryngii play an important role in substrate recognition.

Family S9 prolyl oligopeptidases (POPs) are of interest as pharmacological targets. We recently found that an S9 POP from Pleurotus eryngii showed altered substrate specificity following HO treatment. Oxidation of Met203 on the non-catalytic β-propeller domain resulted in decreased activity toward non-aromatic aminoacyl-para-nitroanilides (pNAs) while maintaining its activity toward aromatic aminoacyl-pNAs.

Loop of Streptomyces Feruloyl Esterase Plays an Important Role in the Enzyme's Catalyzing the Release of Ferulic Acid from Biomass.

Feruloyl esterases (FAEs) are key enzymes required for the production of ferulic acid from agricultural biomass. Previously, we identified and characterized R18, an FAE from NBRC 12852, which showed no sequence similarity to the known FAEs. To determine the region involved in its catalytic activity, we constructed chimeric enzymes using R18 and its homolog (TH2-18) from strain TH-2.

Effect of oxidation of the non-catalytic β-propeller domain on the substrate specificity of prolyl oligopeptidase from Pleurotus eryngii.

Enzymes belonging to the S9 family of prolyl oligopeptidases are of interest because of their pharmacological importance and have a non-catalytic β-propeller domain. In this study, we found that the oxidation of Met203, which lies on surface of the β-propeller domain, leads to change in the substrate specificity of eryngase, an enzyme from Pleurotus eryngii and a member of the S9 family of prolyl oligopeptidases. The activity of eryngase for L-Phe-p-nitroanilide was maintained following hydrogen peroxide treatment but was dramatically reduced for other p-nitroanilide substrates.

Purification, gene cloning, and characterization of γ-butyrobetainyl CoA synthetase from Agrobacterium sp. 525a.

The report is the first of purification, overproduction, and characterization of a unique γ-butyrobetainyl CoA synthetase from soil-isolated Agrobacterium sp. 525a. The primary structure of the enzyme shares 70-95% identity with those of ATP-dependent microbial acyl-CoA synthetases of the Rhizobiaceae family.

Purification and characterization of 4-N-trimethylamino-1-butanol dehydrogenase from Fusarium merismoides var. acetilereum.

From investigation of 60 filamentous fungi, we identified Fusarium merismoides var. acetilereum, which uses 4-N-trimethylamino-1-butanol (TMA-butanol) as the sole source of carbon and nitrogen. The fungus produced NAD(+)-dependent TMA-butanol dehydrogenase (DH) when it was cultivated in medium containing TMA-butanol.

Crystal structure of D-stereospecific amidohydrolase from Streptomyces sp. 82F2 - insight into the structural factors for substrate specificity.

Unlabelled: D-Stereospecific amidohydrolase (DAH) from Streptomyces sp. 82F2, which catalyzes amide bond formation from d-aminoacyl esters and l-amino acids (aminolysis), can be used to synthesize short peptides with a dl-configuration. We found that DAH can use 1,8-diaminooctane and other amino compounds as acyl acceptors in the aminolysis reaction.

Glassin, a histidine-rich protein from the siliceous skeletal system of the marine sponge Euplectella, directs silica polycondensation.

The hexactinellids are a diverse group of predominantly deep sea sponges that synthesize elaborate fibrous skeletal systems of amorphous hydrated silica. As a representative example, members of the genus Euplectella have proved to be useful model systems for investigating structure-function relationships in these hierarchically ordered siliceous network-like composites. Despite recent advances in understanding the mechanistic origins of damage tolerance in these complex skeletal systems, the details of their synthesis have remained largely unexplored.

Functional and structural characteristics of methylmalonyl-CoA mutase from Pyrococcus horikoshii.

Methylmalonyl-CoA mutase (MCM) requires 5'-deoxyadenosylcobalamin (AdoCbl) as a cofactor and is widely distributed in organisms from bacteria and animals. Although genes encoding putative MCMs are present in many archaea, they are separately encoded in large and small subunits. The large and small subunits of archaeal MCM are similar to the catalytic and AdoCbl-binding domains of human MCM, respectively.

Application of two newly identified and characterized feruloyl esterases from Streptomyces sp. in the enzymatic production of ferulic acid from agricultural biomass.

Ferulic acid (FA), a component of hemicellulose in plant cell walls, is a phenolic acid with several potential applications based on its antioxidant properties. Recent studies have shown that feruloyl esterase (FAE) is a key bacterial enzyme involved in FA production from agricultural biomass. In this study, we screened a library of 43 esterases from Streptomyces species and identified two enzymes, R18 and R43, that have FAE activity toward ethyl ferulate.

Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases.

Pleurotus eryngii serine aminopeptidase that has peptide bond formation activity, redesignated as eryngase, was cloned and expressed. Eryngase has a family S9 peptidase unit in the C-terminal region having a catalytic triad of Ser, Asp, and His. In the phylogenetic relations among the subfamilies of family S9 peptidase (S9A, prolyl oligopeptidase; S9B, dipeptidyl peptidase; S9C, acylaminoacyl peptidase; S9D, glutamyl endopeptidase), eryngase existed alone in the neighbor of S9C subfamily.

Alanine-scanning mutation approach for classification of the roles of conserved residues in the activity and substrate affinity of L-carnitine dehydrogenase.

L-Carnitine dehydrogenase (CDH) is as an excellent tool for L-carnitine (L-Car) estimation. To date, four CDHs have been identified, that share 45 % homology of their proteins. Here 42 conserved residues of CDH from Xanthomonas translucens (Xt-CDH) were substituted successively with alanine.

Identification of residues essential for the activity and substrate affinity of L-carnitine dehydrogenase.

Recently, two L-carnitine dehydrogenases from soil isolates Rhizobium sp. (Rs-CDH) and Xanthomonas translucens (Xt-CDH) have demonstrated to exhibit mutually differing affinities toward L-carnitine. To identify residues important for affinity to the substrate, we compared the primary structure of Xt-CDH and Rs-CDH with the recognized 3D structure of 3-hydroxyacyl-CoA dehydrogenase (PDB code: 1F0Y).