DOCSLIB.ORG

A Directly Cross-Linked L-Ornithine-Containing Peptidoglycan in Cell Walls of Spzrochaeta Stenostrepta

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
A Directly Cross-Linked L-Ornithine-Containing Peptidoglycan in Cell Walls of Spzrochaeta Stenostrepta Volume 36, number 1 FEBS LETTERS October 1973 A DIRECTLY CROSS-LINKED L-ORNITHINE-CONTAINING PEPTIDOGLYCAN IN CELL WALLS OF SPZROCHAETA STENOSTREPTA Karl Heinz SCHLEIFER and Ronald JOSEPH Botanisches Institut der Universitiit Miinchen, 8 Miinchen 19, Menzinger Str. 6 7, and Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, Penn. 19140, USA Received July 1973 1. Introduction out according to Primosigh et al. [8]; N-terminal amino acids of peptides were assayed for by the meth- The location of the peptidoglycan as a thin electron- od of Ghuysen et al. [9]. Determination of C-terminal dense layer adjacent and external to the cytoplasmic amino acids was performed by hydrazinolysis with membrane in cells of Spiro&zeta srenostreptu and anhydrous hydrazine as described by Braunitzer [IO]. Spirochaeta litoralis has recently been demonstrated The configuration of amino acids was determined [ 11. The morphology and chemical composition of the enzymatically; that of alanine as described by Larson spirochetal peptidoglycan [l-4] is similar to that of et al. [ 111; that of glutamic acid as described by many Gram-negative bacteria [5, 61 with the exception Niebler et al. [ 121 and that of ornithine as described that L-ornithine [l] occurs as the diamino acid instead by Jones [13]. of either lysine or diaminopimelic acid. Since a new type may occur in these organisms [ 11, we have elucidated the primary structure of the peptidoglycan 3. Results of S. stenostrepa ATCC 25803. The evidence for a directly cross-linked, L-omithine-containing peptido- The quantitative amino acid and amino sugar glycan is presented in this paper. composition, and molar ratios of the peptidoglycan components are listed in table 1. The peptidoglycan was composed solely of glucosamine, muramic acid, 2. Methods ornithine, glutamic acid and alanine. Ammonia release occurred only after total hydrolysis of peptidoglycan The peptidoglycan ofS. stenostrepta ATCC 25083 (less than 0.2 moles/mole of glutamic acid), indicating was isolated as previously described [ 11. The purity that the cr-carboxyl group of glutamic acid was prob- of the peptidoglycan preparation was determined by ably not amidated. Only the alanine content varied electron microscopy and amino acid analysis. Total (1.3 1 - 1.8 moles/mole glutamic acid) depending on hydrolysis of the peptidoglycan and peptides was the peptidoglycan preparation used. A possible explan- carried out in 4 N HCl at 100°C for 16 hr. ation for this diversity will be given later. Isolation of peptides from partial acid hydrolysates Ornithine was present only as the L-isomer, where- of the peptidoglycan and determination of the amino as glutamic acid occurred solely as D-isomer. The ratio acid sequence of these peptides were performed as of L-alanine to D-alanine was 1.0:0.28. Following described previously by Schleifer and Kandler [7]. dinitrophenylation and total acid hydrolysis &DNP- Dinitrophenylation of the peptidoglycan was carried ornithine was the only dinitrophenylated amino acid North-Holland Publishing Company - Amsterdam 83 Volume 36, number 1 FEBS LETTERS October 1913 Table 1 group. Two-dimensional chromatography of a partial Amino acid and amino sugar composition of the peptidoglycan acid hydrolysate of the peptidoglycan was used to of S. stenostreptaa. determine the amino acid sequence (fig. 1, table 2). pmole/mgb Molar ratioC The occurrence of the peptides muramyl-L-alanine, L-alanyl-D-glutamic acid, y-D-glutamyl-L-omithine Muramic acid 0.515 0.99 and L-ornithyl-D&nine established the following Glucosamine 0.492 0.95 sequence in the peptide subunit: muramyl-lalanyl- Glutamic acid 0.521 1.0 y-D-glutamyl-L-omithyl-D-alanine. The occurrence of Alanine 0.682 1.31 the peptide N5-D-alanyl-L-omithine indicated that the Ornithine 0.531 1.02 Ammonia 0.063 0.12 peptide subunits were directly cross-linked between the &amino group of L-ornithine and the carboxyl a Hydrolysis was in 4 N HCI at 100°C for 16 hr. Analysis was group of D-alanine of an adjacent peptide subunit. performed on a Beckman 120C amino acid analyzer. The occurrence of polymerized peptide subunits was b pmole/mg of peptidoglycan. unlikely as the peptides D-alanyl-L-alanine and c Molar ratio relative to glutamic acid. D-alanyl-L-alanyl-D-ghrtamic acid which would be hydrolysis products of such a sequence were not found. Of the total omithine, 68% contained an detected. N-terminal b-amino group and thus 68% of the orni- Only about 30% of the L-ornithine residues were thine residues were not involved in the cross-linkage. involved in the cross-linkage because 68% of the In addition, ornithine was the only C-terminal amino ornithine residues contained an unsubstituted &amino acid in the intact peptidoglycan. At least 60% of the group. This low rate of cross-linkage was also in agree- total ornithine possessed an unsubstituted carboxyl ment with the low content of D-alanine (0.3 moles/ mole glutamic acid). The lack of C-terminal D-alanine residues indicated that all of the D-alanine was involved Isopropanol-aceticocrd-water in cross-linkages. This, in turn, suggested that very potent D-alanyl-D&nine and D-alanine carboxypep- tidases occurred in S. stenostrepta. Because of this the content of D&nine, and thus the total content of alanine and the degree of cross-linkage may vary in different peptidoglycan preparations [ 11. A typical fragment of the proposed primary struc- ture of the peptidoglycan of S. stenostrepa is depicted in fig. 2. As in almost all other peptidoglycans the amino groups of muramic acid and glucosamine were acylated since neither DNP-muramic acid nor DNP- glucosamine were detected in total hydrolysates of dinitrophenylated peptidoglycan. At least 50% of the peptide subunits must consist of the tripeptide IV-acyl-muramyl-L-alanyl-y-D-ghrtamyl-L-ornithine because of the low amount of cross-linkage (30%). Fig. 1. Twodimensional paper chromatogram of a partial acid hydrolysate (4 N HCl, lOO”C, 45 min) of the peptidoglycan of S. stenostrepta. Development was ascending in: i) iso- 4. Discussion propanolPacetic acid-water (75: 10: 1.5, v/v/v) and ii) a-pico- linee25% NH4OH-water (70:2:28, v/v/v); Single hatch, amino The peptidoglycan of S. stenostrepta and possibly acids; cross hatch, peptides; (1) ornithine; (2) glutamic acid; (3) alanine; (4) muramic acid; (5) ghrcosamine; (6) r-D-glut- that of S. Zitoralistoo, are the first known examples amyl-L-ornithine; (7) L-alanyl-D-glutamyl-L-ornithine; (8) L- of a directly cross-linked peptidoglycan containing ornithyl-D-alanine; (9) NS-D-alanyl-L-ornithine; (10) L-alanyl- L-ormthine as diamino acid. For a long time the direct D-glutamic acid; (11) muramyl-L-alanine. 84 Volume 36, number 1 FEBS LETTERS October 1973 MurNAc - -GlcNAc - MurNAc - GlcNAc - 1 1 L-Ala_ L- Ala 1 D-GIu.2, A L-Orn D- Ala T L- Orn L-Orn T ’ D-Glu 1 t L-Ala L- Ala t t -MurNAc - GlcNAc - Mur NAc -GIcNAc - Fig. 2. Proposed primary structure of the peptidoglycan of S. stenostrepm cross-linkage in which the peptide subunits were con- peptidoglycan in Gram-positive bacteria. Thus, the nected without an insertion of additional interpeptide actual difference between the peptidoglycan of bridges seemed to occur only in peptidoglycans con- S. stenostrepta (and probably of other spirochetes) taining meso-diaminopimelic acid. Very recently, and that of Gram-negative Eubacteriales appears only however, Nakkl et al. [ 141 have shown that the same to be in the diamino acid. type of peptide bridging also occurs in peptidoglycans cofitaining L-lysine. In addition to the ultrastructural similarity [I], the chemical structure of the peptido- Acknowledgements glycan of S. sfenosfrepta is similar to that in many Gram- negative eubacteria. The peptide subunits are directly We are indebted to Mrs. G. Niedermeyer and Mrs. cross-linked in both cases, only the diamino acids being L. Hagner for excellent technical assistance. The work different. This monolayered peptidoglycan is rather was supported by the Deutsche Forschnugsgemein- different from the multilayered arrangement of the schaft . Table 2 Amino acid composition and sequence of the peptides of the peptidoglycan of S. stenostrepta. Peptide Molar ratio DNP amino acids Peptide structure no. Ala Gill Om Mur 6 _ 1.0 0.9 _ DNP-Glu, 6-DNP-01x1 r-D-Glu-L-Om I 0.88 1.0 0.95 _ DNP-Ala, 6-DNP-Orn L-Ala- -D-Glu-L-Om 8 1.1 _ 1.0 _ di-DNP-Orn L-Orn-D-Ala 9 1.04 - 1.0 _ 6-DNP-Orn, DNP-Ala NS-D-Ala-L-Orn 10 0.95 1.0 - _ DNP-Ala L-Ala-D-Glu 11 1.0 _ _ 1.1 - Mur-L-Ala 85 Volume 36, number 1 FEBS LETTERS October 1973 References ]8] Primosigh, J., Pelzer, H., Maass, D. and Weidel, W. (1961) Biochim. Biophys. Acta 46, 68. [9] Ghuysen, J.M., Tipper, D.J. and Strominger, J.L. (1966) Joseph, R., Holt, S.C. and Canale-Parola, E. (1973) J. [II in: Methods in Enzymology, Vol. 8, p. 685 (Neufeld, Bacterial. 115, in press. E.F. and Ginsburg, V., eds.), Academic Press, Inc., New Joseph, R. and CanaleParola, E. (1972) Arch. Mikrobiol. PI York. 81, 146. [lo] Braunitzer, G. (1955) Chem. Berichte 88, 2025. Pillot, J. and Ryter, A. (1965) Ann. Inst. Pasteur 108, [31 [ 1 l] Larsen, D.M., Snetsinger, D.C. and Waibel, P.E. (1971) 791. Anal. Biochem. 39, 395. Tinelli, R. and Pillot, J. (1966) Compt. Rend. 263, 739. [41 [12] Niebler, E., Schleifer, K.H. and Kandler, 0.
Load more

Recommended publications
  • Dietary Supplements Compendium 2019 Edition
    Products and Services New Dietary Supplements Reference Standards Below is a list of newly released Reference Standards. Herbal Medicines/ Botanical Dietary Supplements Baicalein Baicalein 7-O-Glucuronide Chebulagic Acid Dietary Supplements Compendium 2019 Edition Coptis chinensis Rhizome Dry Extract In response to the customer feedback, coupled with evolving information needs, USP moved the Psoralen Dietary Supplements Compendium (DSC) to an online platform for the 2019 edition. DSC continues Scutellaria baicalensis Root Dry to provide in-depth, comprehensive information for all phases of development and manufacturing of Extract quality dietary supplements including quality control, quality assurance, and regulatory/compendial Terminalia chebula Fruit Dry affairs. Extract Guarana Seed Dry Extract Some of the advantages that come with the new online DSC edition include: Cullen Corylifolium Fruit Dry Extract More frequent updates to ensure access to the most current information Procyanidin B2 Customizable alerts to notify of changes to selected documents An intuitive interface to facilitate quick and easy navigation Non-Botanicals A customizable workspace with bookmarks, alerts and a viewing history beta-Glycerylphosphorylcholine Convenient, anytime, anywhere access with common browsers Conjugated Linoleic Acids – In addition to selected new and revised monographs and General Chapters from the USP-NF and Triglycerides Food Chemicals Codex issued since the previous 2015 edition, the DSC 2019 features: Creatine Docosahexaenoic Acid 24 new General Chapters Eicosapentaenoic Acid 72 new dietary ingredient and dietary supplement monographs L-alpha- 27 sets of supplementary information for botanical and nonbotanical dietary supplements Glycerophosphorylethanolamine 59 updated botanical HPTLC plates L-alpha- Revised and updated dietary intake comparison tables Glycerylphosphorylcholine Updated Dietary Supplement Verification Program manual Omega-3 Free Fatty Acids Pyrroloquinoline Quinone View this page for more information or to subscribe to the 2019 online DSC.
    [Show full text]
  • The Diagnosis and Management of Ornithine Transcarbamylase Deficiency in Pregnancy: a Case Report
    Perinatal Journal 2011;19(1):23-27 e-Adress: http://www.perinataljournal.com/20110191006 doi:10.2399/prn.11.0191006 The Diagnosis and Management of Ornithine Transcarbamylase Deficiency in Pregnancy: A Case Report Orkun Çetin1, Cihat fien1, Begüm Aydo¤an1, Seyfettin Uluda¤1, ‹pek Dokurel Çetin2, Hakan Erenel1 1Cerrahpafla T›p Fakültesi Kad›n Hastal›klar› ve Do¤um Anabilim Dal›, ‹stanbul, Türkiye 2Cerrahpafla T›p FakültesiÇocuk Sa¤l›¤› ve Hastal›klar› Anabilim Dal›, ‹stanbul Türkiye Abstract Objective: Ornithine transcarbamylase (OTC) deficiency is the most common urea cycle disorder. In our case, we discussed the fol- low up and the management of the OTC deficiency patient, diagnosed during pregnancy. Case: 32-year-old patient, OTC deficiency was diagnosed during pregnancy which was resulted with missed abortion. In the next pregnancy, the patient treated with phenyl butyrate, arginin ornitin lisin and carbamazepine. Coryon villus sampling (CVS) was done in the first trimester. There was not any mutation in the fetal gene locus. In the 39. gestational week, healthy female baby was deliv- ered by caesarean section. Conclusion: OTC deficiency is a rare disease. To make the followup and the management of these patients during pregnancy, may require knowledge and experience about complications. The treatment must be carried out with multidisciplinary approach. The genetic counseling should be given to the family about the prenatal diagnosis of OTC deficiency (CVS, amniosentesis). Keywords: Ornithine transcarbamylase deficiency, pregnancy, prenatal diagnosis, multidisciplinary approach. Gebelikte ornitin transkarbamilaz eksikli¤i tan›s› ve yönetimi: Olgu sunumu Amaç: Ornitin transkarbamilaz (OTC) eksikli¤i, en s›k rastlanan üre döngüsü bozuklu¤udur.
    [Show full text]
  • Characterization of High-Ornithine-Producing Weissella Koreensis DB1 Isolated from Kimchi and Its Application in Rice Bran Fermentation As a Starter Culture
    foods Article Characterization of High-Ornithine-Producing Weissella koreensis DB1 Isolated from Kimchi and Its Application in Rice Bran Fermentation as a Starter Culture Mun So Yeong , Moon Song Hee and Chang Hae Choon * Kimchi Research Center, Department of Food and Nutrition, Chosun University, 309 Pilmun-daero, Dong-gu, Gwangju 61452, Korea; [email protected] (M.S.Y.); [email protected] (M.S.H.) * Correspondence: [email protected] Received: 11 September 2020; Accepted: 23 October 2020; Published: 26 October 2020 Abstract: High-ornithine-producing Weissella koreensis DB1 were isolated from kimchi. Ornithine is produced from arginine via the intracellular arginine deiminase pathway in microorganisms; thus, high cell growth is important for producing ornithine in large quantities. In this study, excellent W. koreensis DB1 growth (A600: 5.15–5.39) was achieved in de Man, Rogosa, and Sharpe (MRS) medium supplemented with 1.0–3.0% arginine (pH 5.0) over 24–48 h at 30 ◦C, and the highest ornithine (15,059.65 mg/L) yield was obtained by culture in MRS containing 3.0% arginine for 48 h. W. koreensis DB1 was further investigated as a functional starter culture for rice bran fermentation. After 48 h of fermentation at 30 ◦C, the fermented rice bran was freeze-dried and ground. The prepared fermented rice bran contained 43,074.13 mg/kg of ornithine and 27,336.37 mg/kg of citrulline, which are used as healthcare supplements due to their beneficial effects. Furthermore, the organoleptic quality of the fermented rice bran was significantly improved, and the fermented product contained viable cells (8.65 log CFU/mL) and abundant dietary fiber.
    [Show full text]
  • Tri-Amino™ Support for Healthy Function of Muscle and Vascular Systems
    PRODUCT DATA DOUGLAS LABORATORIES® 04/2012 1 Tri-Amino™ Support for healthy function of muscle and vascular systems DESCRIPTION Tri-Amino™, provided by Douglas Laboratories, includes significant amounts of the amino acids L-ornithine, L-arginine, and L-lysine. FUNCTIONS Amino acids have many functions in the body. They are the building blocks for all body proteins—structural proteins that build muscle, connective tissues, bones and other structures, and functional proteins in the form of thousands of metabolically active enzymes. Amino acids provide the body with the nitrogen that is essential for growth and maintenance of all tissues and structures. Aside from these general functions, individual amino acids also have specific functions in many aspects of human physiology and biochemistry. L-arginine is a conditionally essential dibasic amino acid. The body is usually capable of producing sufficient amounts of arginine, but in times of physical stress, endogenous synthesis is often inadequate to meet the increased demands. L-arginine can either be used for glucose synthesis or catabolized to produce energy via the tricarboxylic acid cycle. It is also the sole source of nitric oxide (NO), via the enzyme nitric oxide synthase. NO can affect a variety of physiological processes, including relaxation of arterial smooth muscle, platelet aggregation, and neuroendocrine secretion. L-arginine is required for the synthesis of creatine phosphate. Similar to adenosine triphosphate (ATP), creatine phosphate functions as a carrier of readily available energy for contractile work in muscles. Adequate reservoirs of creatine phosphate are necessary in muscle as an energy reserve for anaerobic activity. L-arginine is also a precursor of polyamines, including putrescine, spermine and spermidine.
    [Show full text]
  • Serum Metabolite Profiles As Potential Biochemical Markers in Young
    www.nature.com/scientificreports OPEN Serum metabolite profles as potential biochemical markers in young adults with community- acquired pneumonia cured by moxifoxacin therapy Bo Zhou1, Bowen Lou2,4, Junhui Liu3* & Jianqing She2,4* Despite the utilization of various biochemical markers and probability calculation algorithms based on clinical studies of community-acquired pneumonia (CAP), more specifc and practical biochemical markers remain to be found for improved diagnosis and prognosis. In this study, we aimed to detect the alteration of metabolite profles, explore the correlation between serum metabolites and infammatory markers, and seek potential biomarkers for young adults with CAP. 13 Eligible young mild CAP patients between the ages of 18 and 30 years old with CURB65 = 0 admitted to the respiratory medical department were enrolled, along with 36 healthy participants as control. Untargeted metabolomics profling was performed and metabolites including alcohols, amino acids, carbohydrates, fatty acids, etc. were detected. A total of 227 serum metabolites were detected. L-Alanine, 2-Hydroxybutyric acid, Methylcysteine, L-Phenylalanine, Aminoadipic acid, L-Tryptophan, Rhamnose, Palmitoleic acid, Decanoylcarnitine, 2-Hydroxy-3-methylbutyric acid and Oxoglutaric acid were found to be signifcantly altered, which were enriched mainly in propanoate and tryptophan metabolism, as well as antibiotic-associated pathways. Aminoadipic acid was found to be signifcantly correlated with CRP levels and 2-Hydroxy-3-methylbutyric acid and Palmitoleic acid with PCT levels. The top 3 metabolites of diagnostic values are 2-Hydroxybutyric acid(AUC = 0.90), Methylcysteine(AUC = 0.85), and L-Alanine(AUC = 0.84). The AUC for CRP and PCT are 0.93 and 0.91 respectively.
    [Show full text]
  • Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat
    Pediat. Res. 6: 713-719 (1972) Amino acid neonate intestine transport, amino acid Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat J. F. FITZGERALD1431, S. REISER, AND P. A. CHRISTIANSEN Departments of Pediatrics, Medicine, and Biochemistry, and Gastrointestinal Research Laboratory, Indiana University School of Medicine and Veterans Administration Hospital, Indianapolis, Indiana, USA Extract The activity of amino acid transport pathways in the small intestine of the 2-day-old rat was investigated. Transport was determined by measuring the uptake of 1 mM con- centrations of various amino acids by intestinal segments after a 5- or 10-min incuba- tion and it was expressed as intracellular accumulation. The neutral amino acid transport pathway was well developed with intracellular accumulation values for leucine, isoleucine, valine, methionine, tryptophan, phenyl- alanine, tyrosine, and alanine ranging from 3.9-5.6 mM/5 min. The intracellular accumulation of the hydroxy-containing neutral amino acids threonine (essential) and serine (nonessential) were 2.7 mM/5 min, a value significantly lower than those of the other neutral amino acids. The accumulation of histidine was also well below the level for the other neutral amino acids (1.9 mM/5 min). The basic amino acid transport pathway was also operational with accumulation values for lysine, arginine and ornithine ranging from 1.7-2.0 mM/5 min. Accumulation of the essential amino acid lysine was not statistically different from that of nonessential ornithine. Ac- cumulation of aspartic and glutamic acid was only 0.24-0.28 mM/5 min indicating a very low activity of the acidic amino acid transport pathway.
    [Show full text]
  • Waste Nitrogen Excretion Via Amino Acid Acylation: Benzoate and Phenylacetate in Lysinuric Protein Intolerance
    003 1-39981861201 1- 1 1 17$02.00/0 PEDIATRIC RESEARCH Vol. 20, No. 11, 1986 Copyright O 1986 International Pediatric Research Foundation. Inc Prinled in (I.S. A. Waste Nitrogen Excretion Via Amino Acid Acylation: Benzoate and Phenylacetate in Lysinuric Protein Intolerance OLLl SIMELL, ILKKA SIPILA, JUKKA RAJANTIE, DAVID L. VALLE, AND SAUL W. BRUSILOW CXildren '.Y Hospital, Universitj9ofl-lelsinki, SF-00290 Helsinki, Finland; and Department of'Pediatrics, The Johns Hopkins Unive,siij~School of Medicine, Baltimore, Maryland 21205 ABSTRACT. Benzoate and phenylacetate improve prog- glutamine, respectively; less than 3.5% appeared un- nosis in inherited urea cycle enzyme deficiencies by increas- changed in urine. (Pediatr Res 20: 1117-1 121, 1986) ing waste nitrogen excretion as amino acid acylation prod- ucts. We studied metabolic changes caused by these sub- Abbreviations stances and their pharmacokinetics in a biochemically different urea cycle disorder, lysinuric protein intolerance LPI, lysinuric protein intolerance (LPI), under strictly standardized induction of hyperam- iv, intravenous monemia. Five patients with LPI received an intravenous infusion of 6.6 mmol/kg L-alanine alone and separately with 2.0 mmollkg of benzoate or phenylacetate in 90 min. Blood for ammonia, serum urea and creatinine, plasma In 19 14, Lewis (I) showed that benzoate modifies waste nitro- benzoate, hippurate, phenylacetate, phenylacetylgluta- gen excretion by decreasing production of urea via excretion of mine, and amino acids was obtained at 0, 120, 180, and waste nitrogen as the acylation product of glycine with benzoate, 270 min. Urine was collected in four consecutive 6-h pe- i.e. hippurate. A few years later (2) phenylacetate was noted to riods.
    [Show full text]
  • L-Citrulline Supplementation: Impact on Cardiometabolic Health
    nutrients Review L-Citrulline Supplementation: Impact on Cardiometabolic Health Timothy D. Allerton 1, David N. Proctor 2, Jacqueline M. Stephens 1, Tammy R. Dugas 3, Guillaume Spielmann 1,4 and Brian A. Irving 1,4,* ID 1 Pennington Biomedical Research Center, Baton Rouge, LA 70808, USA; [email protected] (T.D.A.); [email protected] (J.M.S.); [email protected] (G.S.) 2 Department of Kinesiology, Pennsylvania State University, University Park, PA 16802, USA; [email protected] 3 Department of Comparative Biomedical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, USA; [email protected] 4 Department of Kinesiology, Louisiana State University, Baton Rouge, LA 70803, USA * Correspondence: [email protected]; Tel.: +1-225-578-7179; Fax: 225-578-3680 Received: 20 June 2018; Accepted: 16 July 2018; Published: 19 July 2018 Abstract: Diminished bioavailability of nitric oxide (NO), the gaseous signaling molecule involved in the regulation of numerous vital biological functions, contributes to the development and progression of multiple age- and lifestyle-related diseases. While L-arginine is the precursor for the synthesis of NO by endothelial-nitric oxide synthase (eNOS), oral L-arginine supplementation is largely ineffective at increasing NO synthesis and/or bioavailability for a variety of reasons. L-citrulline, found in high concentrations in watermelon, is a neutral alpha-amino acid formed by enzymes in the mitochondria that also serves as a substrate for recycling L-arginine. Unlike L-arginine, L-citrulline is not quantitatively extracted from the gastrointestinal tract (i.e., enterocytes) or liver and its supplementation is therefore more effective at increasing L-arginine levels and NO synthesis.
    [Show full text]
  • The Protective Role of Alpha-Ketoglutaric Acid on the Growth and Bone Development of Experimentally Induced Perinatal Growth-Retarded Piglets
    animals Article The Protective Role of Alpha-Ketoglutaric Acid on the Growth and Bone Development of Experimentally Induced Perinatal Growth-Retarded Piglets Ewa Tomaszewska 1,* , Natalia Burma ´nczuk 1, Piotr Dobrowolski 2 , Małgorzata Swi´ ˛atkiewicz 3 , Janine Donaldson 4, Artur Burma ´nczuk 5, Maria Mielnik-Błaszczak 6, Damian Kuc 6, Szymon Milewski 7 and Siemowit Muszy ´nski 7 1 Department of Animal Physiology, Faculty of Veterinary Medicine, University of Life Sciences in Lublin, Akademicka St. 12, 20-950 Lublin, Poland; [email protected] 2 Department of Functional Anatomy and Cytobiology, Faculty of Biology and Biotechnology, Maria Curie-Sklodowska University, Akademicka St. 19, 20-033 Lublin, Poland; [email protected] 3 Department of Animal Nutrition and Feed Science, National Research Institute of Animal Production, Krakowska St. 1, 32-083 Balice, Poland; [email protected] 4 Faculty of Health Sciences, School of Physiology, University of the Witwatersrand, 7 York Road, Parktown, Johannesburg 2193, South Africa; [email protected] 5 Faculty of Veterinary Medicine, Institute of Preclinical Veterinary Sciences, University of Life Sciences in Lublin, Akademicka St. 12, 20-950 Lublin, Poland; [email protected] 6 Department of Developmental Dentistry, Medical University of Lublin, 7 Karmelicka St., 20-081 Lublin, Poland; [email protected] (M.M.-B.); [email protected] (D.K.) 7 Department of Biophysics, Faculty of Environmental Biology, University of Life Sciences in Lublin, Citation: Tomaszewska, E.; Akademicka St. 13, 20-950 Lublin, Poland; [email protected] (S.M.); [email protected] (S.M.) Burma´nczuk,N.; Dobrowolski, P.; * Correspondence: [email protected] Swi´ ˛atkiewicz,M.; Donaldson, J.; Burma´nczuk,A.; Mielnik-Błaszczak, Simple Summary: Perinatal growth restriction is a significant health issue that predisposes to M.; Kuc, D.; Milewski, S.; Muszy´nski, S.
    [Show full text]
  • Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Pinus Pinaster Ait.)
    plants Article Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Pinus pinaster Ait.) José Alberto Urbano-Gámez, Jorge El-Azaz, Concepción Ávila , Fernando N. de la Torre * and Francisco M. Cánovas * Grupo de Biología Molecular y Biotecnología, Departamento de Biología Molecular y Bioquímica, Universidad de Málaga, Campus Universitario de Teatinos, 29071 Málaga, Spain; [email protected] (J.A.U.-G.); [email protected] (J.E.-A.); [email protected] (C.Á.) * Correspondence: [email protected] (F.N.d.l.T.); [email protected] (F.M.C.) Received: 11 September 2020; Accepted: 24 September 2020; Published: 27 September 2020 Abstract: The amino acids arginine and ornithine are the precursors of a wide range of nitrogenous compounds in all living organisms. The metabolic conversion of ornithine into arginine is catalyzed by the sequential activities of the enzymes ornithine transcarbamylase (OTC), argininosuccinate synthetase (ASSY) and argininosuccinate lyase (ASL). Because of their roles in the urea cycle, these enzymes have been purified and extensively studied in a variety of animal models. However, the available information about their molecular characteristics, kinetic and regulatory properties is relatively limited in plants. In conifers, arginine plays a crucial role as a main constituent of N-rich storage proteins in seeds and serves as the main source of nitrogen for the germinating embryo. In this work, recombinant PpOTC, PpASSY and PpASL enzymes from maritime pine (Pinus pinaster Ait.) were produced in Escherichia coli to enable study of their molecular and kinetics properties. The results reported here provide a molecular basis for the regulation of arginine and ornithine metabolism at the enzymatic level, suggesting that the reaction catalyzed by OTC is a regulatory target in the homeostasis of ornithine pools that can be either used for the biosynthesis of arginine in plastids or other nitrogenous compounds in the cytosol.
    [Show full text]
  • The Role of Glutamine and Α-Ketoglutarate in Gut Metabolism and the Potential Application in Medicine and Nutrition Rafał Filip1, Stefan G
    Journal of Pre-Clinical and Clinical Research, Vol 1, No 1, 009-015 REVIEW www.jpccr.eu The role of glutamine and α-ketoglutarate in gut metabolism and the potential application in medicine and nutrition Rafał Filip1, Stefan G. Pierzynowski2 1 Department of Endoscopy & Department of Internal and Occupational Diseases, Institute of Agricultural Medicine, Lublin, Poland 2 Department of Cell and Organism Biology, Lund University, Lund, Sweden Abstract: An amino acid, Glutamine (Gln), is abundant in both the human body and diet. Gln and its derivatives are important factors affecting intestinal function, growth and development as a main source for energy and structure component. The importance to metabolism is evident during stress. During the past 2 decades, an increased understanding has been gained into its role in metabolism. Gln is currently classified as a conditionally essential amino acid; however, it is unstable in water solution and produces toxic byproducts on decomposition, which has led to the commercialization of its precursor - AKG. Apart from its nutritive role, Gln and AKG possess certain pharmacologic and/or immunologic effects. The article presents the role of Gln and AKG in gut metabolism and, on the basis of clinical trials and animal experiments, discusses their potential usefulness in medicine and nutrition. Key words: alpha-ketoglutarate, glutamine, nutrition INTRODUCTION quantity of different toxins [7]. They are not taken in by the intestine because of the presence of the mucosal barrier, In situations such as extensive weight reduction, intensive which consists of three parts: mechanical, biological and exercise, different illnesses or trauma, surgery, quantitative immnunological. Any etiological factors that impair these changes in nutritional intake may not be sufficient or in barriers would cause bacterial/endotoxin translocation [8].
    [Show full text]
  • Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria
    Journal of General Microbiology (1987), 133, 2487-2495. Printed in Great Britain 2487 Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria By VICTOR STALON,l* CORINNE VANDER WAUVEN,2 PATRICIA MOMIN' AND CHRISTIANE LEGRAIN2 Laboratoire de Microbiologie, Universitk Libre de Bruxelles and Institut de Recherches du CERIA, I, avenue E. Gryson, B-1070 Brussels, Belgium (Received 5 January 1987; revised 13 April 1987) ~~ ~~ ~ ~ ~~ ~ The distribution of the arginine succinyltransferase pathway was examined in representative strains of Pseudomonas and related bacteria able to use arginine as the sole carbon and nitrogen source for growth. The arginine succinyltransferase pathway was induced in arginine-grown cells. The accumulation of succinylornithine following in vivo inhibition of succinylornithine transaminase activity by aminooxyacetic acid showed that this pathway is responsible for the dissimilation of the carbon skeleton of arginine. Catabolism of citrulline as a carbon source was restricted to relatively few of the organisms tested. In P. putida, P. cepacia and P. indigofera, ornithine was the main product of citrulline degradation. In most strains which possessed the arginine succinyltransferase pathway, the first step of ornithine utilization as a carbon source was the conversion of ornithine into succinylornithine through an ornithine succinyltransferase. However P. cepacia and P.putida used ornithine by a pathway which proceeded via proline as an intermediate and involved an ornithine cyclase activity. INTRODUCTION Bacterial species utilize arginine through various pathways (for a review see Cunin et al., 19863). The guanidino group of arginine is subject to either hydrolytic cleavage by arginase to form ornithine and urea or to deamination, producing citrulline and ammonia.
    [Show full text]