| |||
Biosynthetic Route (biosynthetic + route)
Selected AbstractsStructural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway , evidence of a different substrate specificityFEBS JOURNAL, Issue 21 2009Nicola Barison HP1287 (tenA) from Helicobacter pylori is included among the genes that play a relevant role in bacterium colonization and persistence. The gene has been cloned and its product, protein TenA, has been expressed and purified. The crystal structures of the wild-type protein and the mutant F47Y have been determined at resolutions of 2.7 and 2.4 Å, respectively. The molecular model, a homotetramer with 222 symmetry, shows that the H. pylori TenA structure belongs to the thiaminase II class of proteins. These enzymes were recently found to be involved in a salvage pathway for the synthesis of the thiamin precursor hydroxypyrimidine, which constitutes a building block in thiamin biosynthesis, in particular in bacteria living in the soil. By contrast, enzymatic measurements on TenA from H. pylori indicate that the activity on the putative substrate 4-amino-5-aminomethyl-2-methylpyrimidine is very modest. Moreover, in the present study, we demonstrate that the mutation at residue 47, a position where a phenylalanine occurs in all the strains of H. pylori sequenced to date, is not sufficient to explain the very low catalytic activity toward the expected substrate. As a result of differences in the colonization environment of H. pylori as well as the TenA structural and catalytic peculiar features, we suggest a possible pivotal role for the H. pylori enzyme in the thiamin biosynthetic route, which is in agreement with the relevance of this protein in the stomach colonization process. Structured digital abstract ,,MINT-7260232: TenA (uniprotkb:O25874) and TenA (uniprotkb:O25874) bind (MI:0407) by x-ray crystallography (MI:0114) [source] Acetyl-CoA:1- O -alkyl- sn -glycero-3-phosphocholine acetyltransferase (lyso-PAF AT) activity in cortical and medullary human renal tissueFEBS JOURNAL, Issue 14 2003Tzortzis N Nomikos Platelet-activating factor (PAF) is one of the most potent inflammatory mediators. It is biosynthesized by either the de novo biosynthesis of glyceryl ether lipids or by remodeling of membrane phospholipids. PAF is synthesized and catabolized by various renal cells and tissues and exerts a wide range of biological activities on renal tissue suggesting a potential role during renal injury. The aim of this study was to identify whether cortex and medulla of human kidney contain the acetyl-CoA:1- O -alkyl- sn -glycero-3-phosphocholine acetyltransferase (lyso-PAF AT) activity which catalyses the last step of the remodeling biosynthetic route of PAF and is activated in inflammatory conditions. Cortex and medulla were obtained from nephrectomized patients with adenocarcinoma and the enzymatic activity was determined by a trichloroacetic acid precipitation method. Lyso-PAF AT activity was detected in both cortex and medulla and distributed among the membrane subcellular fractions. No statistical differences between the specific activity of cortical and medullary lyso-PAF AT was found. Both cortical and medullary microsomal lyso-PAF ATs share similar biochemical properties indicating common cellular sources. [source] Living Yeast Cells as a Controllable Biosynthesizer for Fluorescent Quantum DotsADVANCED FUNCTIONAL MATERIALS, Issue 15 2009Ran Cui Abstract There are currently some problems in the field of chemical synthesis, such as environmental impact, energy loss, and safety, that need to be tackled urgently. An interdisciplinary approach, based on different backgrounds, may succeed in solving these problems. Organisms can be chosen as potential platforms for materials fabrication, since biosystems are natural and highly efficient. Here, an example of how to solve some of these chemical problems through biology, namely, through a novel biological strategy of coupling intracellular irrelated biochemical reactions for controllable synthesis of multicolor CdSe quantum dots (QDs) using living yeast cells as a biosynthesizer, is demonstrated. The unique fluorescence properties of CdSe QDs can be utilized to directly and visually judge the biosynthesis phase to fully demonstrate this strategy. By such a method, CdSe QDs, emitting at a variety of single fluorescence wavelengths, can be intracellularly, controllably synthesized at just 30°C instead of at 300°C with combustible, explosive, and toxic organic reagents. This green biosynthetic route is a novel strategy of coupling, with biochemical reactions taking place irrelatedly, both in time and space. It involves a remarkable decrease in reaction temperature, from around 300 °C to 30 °C and excellent color controllability of CdSe photoluminescence. It is well known that to control the size of nanocrystals is a mojor challenge in the biosynthesis of high-quality nanomaterials. The present work demonstrates clearly that biological systems can be creatively utilized to realize controllable unnatural biosynthesis that normally does not exist, offering new insights for sustainable chemistry. [source] Structural analysis of 3-,-acetyl-20(29)-lupene-24-oic acid, a novel pentacyclic triterpene isolated from the gum resin of Boswellia serrata, by NMR spectroscopyMAGNETIC RESONANCE IN CHEMISTRY, Issue 8 2003Klaus Belsner Abstract 3,-Acetyl-20(29)-lupene-24-oic acid (1) was isolated from the gum resin of Boswellia serrata. Its presence evidently suggests, that the oxidosqualene triterpene pathway of Boswellia serrata closely resembles the biosynthetic route already found in other plants. Complete 1H and 13C spectral assignments were derived from 1D and 2D NMR spectra. This is the first compound with the lupene backbone combining a 3,-hydroxy or 3,-acetyl group with the 24-carboxyl group, a configuration which is typical of the classical boswellic acids. Copyright © 2003 John Wiley & Sons, Ltd. [source] Crystallization and preliminary crystallographic characterization of GumK, a membrane-associated glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesisACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2006Máximo Barreras GumK is a membrane-associated inverting glucuronosyltransferase that is part of the biosynthetic route of xanthan, an industrially important exopolysaccharide produced by Xanthomonas campestris. The enzyme catalyzes the fourth glycosylation step in the pentasaccharide-P-P-polyisoprenyl assembly, an oligosaccharide diphosphate lipid intermediate in xanthan biosynthesis. GumK has marginal homology to other glycosyltransferases (GTs). It belongs to the CAZy family GT 70, for which no structure is currently available, and indirect biochemical evidence suggests that it also belongs to the GT-B structural superfamily. Crystals of recombinant GumK from X. campestris have been grown that diffract to 1.9,Å resolution. Knowledge of the crystal structure of GumK will help in understanding xanthan biosynthesis and its regulation and will also allow a subsequent rational approach to enzyme design and engineering. The multiwavelength anomalous diffraction approach will be used to solve the phase problem. [source] Chemical synthesis and biosynthesis of the cyclotide family of circular proteinsIUBMB LIFE, Issue 9 2006Sunithi Gunasekera Abstract Cyclotides are a recently discovered class of proteins that have a characteristic head-to-tail cyclized backbone stabilized by a knotted arrangement of three disulfide bonds. They are exceptionally resistant to chemical, enzymatic and thermal treatments because of their unique structural scaffold. Cyclotides have a range of bio-activities, including uterotonic, anti-HIV, anti-bacterial and cytotoxic activity but their insecticidal properties suggest that their natural physiological role is in plant defense. They are genetically encoded as linear precursors and subsequently processed to produce mature cyclic peptides but the mechanism by which this occurs remains unknown. Currently most cyclotides are obtained via direct extraction from plants in the Rubiaceae and Violaceae families. To facilitate the screening of cyclotides for structure-activity studies and to exploit them in drug design or agricultural applications a convenient route for the synthesis of cyclotides is vital. In this review the current chemical, recombinant and biosynthetic routes to the production of cyclotides are discussed. iubmb Life, 58: 515-524, 2006 [source] Biosynthetic pathways of the pheromone of the Egyptian armyworm Spodoptera littoralisPHYSIOLOGICAL ENTOMOLOGY, Issue 4 2008LOURDES MUÑOZ Abstract Most insect pheromones comprise multicomponent blends of geometric or optical isomers, and one major question is how insects produce species-specific ratios of components for successful reproductive isolation. Key enzymes suggested to be involved in pheromone biosynthesis are acetyl-coenzyme A carboxylase and fatty acyl synthetase, chain-shortening enzymes, desaturases, elongases, reductases, oxidases, and alcohol acetyl transferases. The female pheromone composition of the Egyptian armyworm Spodoptera littoralis (Boisd.) is highly dependent on the origin of the strain. In this review, we present a summary of the different reported pheromone compositions of the moth, including from our recent studies on this subject, as well as the biosynthetic routes to the different components and the molecular approaches involved. In addition, the key role played in the proposed biosynthetic pathways by a number of important biosynthetic enzymes, such as chain shortening enzymes, desaturases and alcohol acetyl transferases, is outlined, as well as the latest developments on the inhibition of these enzymes. [source] Labeled brassinosteroids for biochemical studiesTHE CHEMICAL RECORD, Issue 5 2007Vladimir Khripach Abstract The present paper describes the results of our studies on the synthesis of brassinolide biosynthetic precursors as tools for investigations of new biosynthetic routes leading to brassinosteroids. The corresponding labeled compounds containing three or six deuterium atoms at terminal methyl group(s) of the side chain (in a position ensuring lack of isotopic exchange) were prepared starting from stigmasterol or bisnorcholenic acid. Two strategies for the construction of the carbon skeleton of the side chain were applied in this study: Claisen rearrangement of allylic alcohols and convergent synthesis based on the coupling of 22-aldehydes with appropriate chiral sulfone. More than 20 brassinolide precursors (actual or suspected) have been prepared for metabolic studies that enabled identification of new brassinosteroids and biosynthetic subpathways to brassinolide in Secale cereale and Arabidopsis thaliana. © 2007 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 7: 265,274; 2007: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr.20123 [source] |