Biochemistry Centennial Celebration 1915 - 2015
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Collagen and Elastin Fibres
J Clin Pathol: first published as 10.1136/jcp.s3-12.1.49 on 1 January 1978. Downloaded from J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 49-58 Collagen and elastin fibres A. J. BAILEY From the Agricultural Research Council, Meat Research Institute, Langford, Bristol Although an understanding of the intracellular native collagen was generated from type I pro- biosynthesis of both collagen and elastin is of collagen. Whether this means that the two pro- considerable importance it is the subsequent extra- collagens are converted by different enzyme systems cellular changes involving fibrogenesis and cross- and the type III enzyme was deficient in these linking that ensure that these proteins ultimately fibroblast cultures, or that the processing of pro become the major supporting tissues of the body. type III is extremely slow, is not known. The latter This paper summarises the formation and stability proposal is consistent with the higher proportion of collagen and elastin fibres. of soluble pro type III extractable from tissue (Lenaers and Lapiere, 1975; Timpl et al., 1975). Collagen Basement membrane collagens, on the other hand, do not form fibres and this property may be The non-helical regions at the ends of the triple due to the retention of the non-helical extension helix of procollagen probably provide a number of peptides (Kefalides, 1973). In-vivo biosynthetic different intracellular functions-that is, initiating studies showing the absence of any extension peptide rapid formation of the triple helix; inhibiting intra- removal support this (Minor et al., 1976), but other cellular fibrillogenesis; and facilitating transmem- workers have reported that there is some cleavage brane movement. -
01. Amino Acids
01. Amino Acids 1 Biomolecules • Protein • Carbohydrate • Nucleic acid • Lipid 2 peptide polypeptide protein di-, tri-, oligo- 3 4 fibrous proteins proteins globular proteins 5 Figure 4.1 Anatomy of an amino acid. Except for proline and its derivatives, all of the amino acids commonly found in proteins possess this type of structure. 6 Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V)* Leucine (Leu, L)* Isoleucine (Ile. I)* 7 Serine (Ser, S) Threonine (Thr, T)* Cysteine (Cys, C)cystine Methionine (Met, M)* 8 Aspartate (Asp, D) Glutamate (Glu, E) Asparagine (Asn, N) Glutamine (Gln, Q) 9 Lysine (Lys, K)* Arginine (Arg, R)* 10 Phenylalanine (Phe, F)* Tyrosine (Tyr, Y) Histidine (His, H)* Tryptophan (Trp, W)* 11 Proline (Pro, P) 12 Hydrophobic (A, G, I, L, F, V, P) Hydrophilic (D, E, R, S, T, C, N, Q, H) Amphipathic (K, M, W, Y) 13 Essential amino acids: V, L, I, T, M, K, R, F, H, W 14 Several Amino Acids Occur Rarely in Proteins We'll see some of these in later chapters • Selenocysteine in many organisms • Pyrrolysine in several archaeal species • Hydroxylysine, hydroxyproline - collagen • Carboxyglutamate - blood-clotting proteins • Pyroglutamate – in bacteriorhodopsin • GABA, epinephrine, histamine, serotonin act as neurotransmitters and hormones • Phosphorylated amino acids – a signaling device Several Amino Acids Occur Rarely in Proteins Several Amino Acids Occur Rarely in Proteins Figure 4.4 (b) Some amino acids are less common, but nevertheless found in certain proteins. Hydroxylysine and hydroxyproline are found in connective-tissue proteins; carboxy- glutamate is found in blood-clotting proteins; pyroglutamate is found in bacteriorhodopsin (see Chapter 9). -
Collagen Structural Microheterogeneity and a Possible Role for Glycosylated Hydroxylysine in Type 1 Collagen
Proc. NatL Acad. Sci. USA Vol. 79, pp. 7684-7688, December 1982 Biochemistry Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type 1 collagen (nonreducible stable crosslinks/hydroxyaldolhistidine/specific cleavage/molecular location) MITSUO YAMAUCHI*t, CLAUDIA NOYES*t, YOSHINORI KUBOKI*t, AND GERALD L. MECHANIC*§¶ *Dental Research Center, §Department of Biochemistry and Nutrition, and tDepartment of Medicine, University of North Carolina, Chapel Hill, North Carolina 27514 Communicated by. Ernest L. Eliel, September 20, 1982 ABSTRACT A three-chained peptide from type I collagen, and Mechanic (8) that dehydro-HisOHMerDes, which was crosslinked by hydroxyaldolhistidine, has been isolated from a thought to be artifactual (9, 10) is a true crosslink in collagen tryptic digest of5 M guanidine HCI-insoluble bovine skin collagen fibrils. Bernstein and Mechanic found that one HisOHMerDes (a small but as yet unknown percentage of the total collagen in crosslink was present per molecule of collagen in freshly re- whole skin). Os04/NaIO4 specifically cleaved the crosslink at its constituted soluble collagen fibrils. double bond into a two-chained crosslink peptide and a single pep- Histidine was also found to be a constituent of the stable tide. The sequence of the two-chained peptide containing the bi- nonreducible trifunctional crosslink hydroxyaldolhistidine functional crosslink was determined after amino acid analysis of (OHAlHis), whose structure was elucidated by PMR and mass the separated peptides. The crosslink consists of an aldehyde de- spectrometry rived from hydroxylysine-87 in the aldehyde-containing cyanogen (11). OHAIHis was isolated from bovine skin col- bromide fragment alCB5ald and an aldehyde derived from the lagen. -
United States Patent (19) 11 Patent Number: 5,874,589 Campbell Et Al
USOO5874589A United States Patent (19) 11 Patent Number: 5,874,589 Campbell et al. 45) Date of Patent: Feb. 23, 1999 54 METHODS FOR SYNTHESIZING DIVERSE El Marini et al., 1992, Synthesis pp. 1104-1108 Synthesis of COLLECTIONS OF TETRAMIC ACIDS AND enantiomerically pure B-and Y-amino acids from aspartic DERVATIVES THEREOF and glutamic acid derivatives. Evans et al., 1982, J. Amer. Chem. Soc. 104: 1737–1739 75 Inventors: David A. Campbell, San Mateo; Todd Asymmetric alkylation reactions of chiral imide enolates. A T. Romoff, San Jose, both of Calif. practical approach to the enantioselective Synthesis of C-Substituted carboxylic acid derivatives. 73 Assignee: GlaxoWellcome, Inc., Research Fontenot et al., 1991, Peptide Research, 4: 19-25A Survey Triangle Park, N.C. of potential problems and qulaity control in peptide Synthe sis by the flourenylmethocvarbonyl procedure. 21 Appl. No.: 896,799 Giesemann et al., 1982, J. Chem. Res. (S) pp. 79 Synthesis 22 Filed: Jul.18, 1997 of chiral C-isocyano esters and other base-Sensitive isocya nides with 51) Int. Cl. ........................ C07D 211/40; CO7D 207/00 oxomethylenebis-(3H-Imidazolium)Bis(methanesulphonate), 52 U.S. Cl. ............ ... 548/540; 546/220; 548/539 a versatile dehydrating reagent. 58 Field of Search ............................. 546/220; 548/539, Geysen et al., 1987, J. Immunol. Meth. 102: 259-274 548/540 Strategies for epitope analysis using peptide Synthesis. Giron-Forest et al., 1979, Analytical Profiles of Drug Sub 56) References Cited stances, 8: 47-81 Bromocriptine methaneSulphonate. U.S. PATENT DOCUMENTS Gokeletal, 1971, Isonitrile Chemistry, Ugi, I. ed., Academic 3,299.095 1/1967 Harris et al. -
Metatranscriptomic Analysis of Community Structure And
School of Environmental Sciences Metatranscriptomic analysis of community structure and metabolism of the rhizosphere microbiome by Thomas Richard Turner Submitted in partial fulfilment of the requirement for the degree of Doctor of Philosophy, September 2013 This copy of the thesis has been supplied on condition that anyone who consults it is understood to recognise that its copyright rests with the author and that use of any information derived there from must be in accordance with current UK Copyright Law. In addition, any quotation or extract must include full attribution. i Declaration I declare that this is an account of my own research and has not been submitted for a degree at any other university. The use of material from other sources has been properly and fully acknowledged, where appropriate. Thomas Richard Turner ii Acknowledgements I would like to thank my supervisors, Phil Poole and Alastair Grant, for their continued support and guidance over the past four years. I’m grateful to all members of my lab, both past and present, for advice and friendship. Graham Hood, I don’t know how we put up with each other, but I don’t think I could have done this without you. Cheers Salt! KK, thank you for all your help in the lab, and for Uma’s biryanis! Andrzej Tkatcz, thanks for the useful discussions about our projects. Alison East, thank you for all your support, particularly ensuring Graham and I did not kill each other. I’m grateful to Allan Downie and Colin Murrell for advice. For sequencing support, I’d like to thank TGAC, particularly Darren Heavens, Sophie Janacek, Kirsten McKlay and Melanie Febrer, as well as John Walshaw, Mark Alston and David Swarbreck for bioinformatic support. -
Ihyd-Pseaac: Predicting Hydroxyproline and Hydroxylysine in Proteins by Incorporating Dipeptide Position-Specific Propensity Into Pseudo Amino Acid Composition
Int. J. Mol. Sci. 2014, 15, 7594-7610; doi:10.3390/ijms15057594 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Article iHyd-PseAAC: Predicting Hydroxyproline and Hydroxylysine in Proteins by Incorporating Dipeptide Position-Specific Propensity into Pseudo Amino Acid Composition Yan Xu 1,5,*, Xin Wen 1, Xiao-Jian Shao 2, Nai-Yang Deng 3 and Kuo-Chen Chou 4,5 1 Department of Information and Computer Science, University of Science and Technology Beijing, Beijing 100083, China; E-Mail: [email protected] 2 Department of Mathematics and Information Science, Binzhou University, Binzhou 256603, China; E-Mail: [email protected] 3 College of Science, China Agricultural University, Beijing 100083, China; E-Mail: [email protected] 4 Center of Excellence in Genomic Medicine Research (CEGMR), King Abdulaziz University, Jeddah 21589, Saudi Arabia; E-Mail: [email protected] 5 Gordon Life Science Institute, Boston, MA 02478, USA * Author to whom correspondence should be addressed; E-Mail: [email protected] or [email protected]; Tel./Fax: +86-10-6233-2589. Received: 7 February 2014; in revised form: 4 April 2014 / Accepted: 17 April 2014 / Published: 5 May 2014 Abstract: Post-translational modifications (PTMs) play crucial roles in various cell functions and biological processes. Protein hydroxylation is one type of PTM that usually occurs at the sites of proline and lysine. Given an uncharacterized protein sequence, which site of its Pro (or Lys) can be hydroxylated and which site cannot? This is a challenging problem, not only for in-depth understanding of the hydroxylation mechanism, but also for drug development, because protein hydroxylation is closely relevant to major diseases, such as stomach and lung cancers. -
Lysyl-Protocollagen Hydroxylase Deficiency in Fibroblasts from Siblings with Hydroxylysine-Deficient Collagen
Proc. Nat. Acad. Sci. USA Vol. 69, No. 10, pp. 2899-2903, October 1972 Lysyl-Protocollagen Hydroxylase Deficiency in Fibroblasts from Siblings with Hydroxylysine-Deficient Collagen (prolyl-protocollagen hydroxylase/connective tissue/inborn error/crosslinks) S. M. KRANE, S. R. PINNELL, AND R. W. ERBE Departments of Medicine, Dermatology, and Pediatrics, Harvard Medical School and the Medical, Dermatology, and Children's Services, Massachusetts General Hospital, Boston, Massachusetts 02114 Communicated by E. R. Blout, July 31, 1972 ABSTRACT Cell culture studies were performed on were normal. The hydroxylysine content of dermis was also members of a family in which two sisters, ages 9 and 12, normal in three patients, each with the Marfan and Ehlers- have a similar disorder characterized clinically by severe scoliosis, joint laxity and recurrent dislocations, hyper- Danlos syndromes. Collagen from the skin of the affected extensible skin, and thin scars. The skin collagen from the children was more soluble in denaturing solvents than that sisters was markedly deficient in hydroxylysine, but other derived from controls (4), consistent with a defect in cross- amino acids were present in normal amounts. Hydroxy- linking of collagen molecules, a process in which hydroxylysine lysine in collagen from fascia and bone was reduced to a to involved lesser extent. Since the most likely explanation for the has been thought be critically (2, 5-8). Hydroxyly- hydroxylysihie deficiency was a reduction in enzymatic sine per se is not used in collagen biosynthesis; specific lysyl hydroxylation of lysine residues in protocollagen, we mea- residues are hydroxylated after their incorporation into the sured the activity of lysyl-protocollagen hydroxylase in polypeptide chains of protocollagen (9-12). -
Protein Engineering of a Dye Decolorizing Peroxidase from Pleurotus Ostreatus for Efficient Lignocellulose Degradation
Protein Engineering of a Dye Decolorizing Peroxidase from Pleurotus ostreatus For Efficient Lignocellulose Degradation Abdulrahman Hirab Ali Alessa A thesis submitted in partial fulfilment of the requirements for the degree of Doctor of Philosophy The University of Sheffield Faculty of Engineering Department of Chemical and Biological Engineering September 2018 ACKNOWLEDGEMENTS Firstly, I would like to express my profound gratitude to my parents, my wife, my sisters and brothers, for their continuous support and their unconditional love, without whom this would not be achieved. My thanks go to Tabuk University for sponsoring my PhD project. I would like to express my profound gratitude to Dr Wong for giving me the chance to undertake and complete my PhD project in his lab. Thank you for the continuous support and guidance throughout the past four years. I would also like to thank Dr Tee for invaluable scientific discussions and technical advices. Special thanks go to the former and current students in Wong’s research group without whom these four years would not be so special and exciting, Dr Pawel; Dr Hossam; Dr Zaki; Dr David Gonzales; Dr Inas,; Dr Yomi, Dr Miriam; Jose; Valeriane, Melvin, and Robert. ii SUMMARY Dye decolorizing peroxidases (DyPs) have received extensive attention due to their biotechnological importance and potential use in the biological treatment of lignocellulosic biomass. DyPs are haem-containing peroxidases which utilize hydrogen peroxide (H2O2) to catalyse the oxidation of a wide range of substrates. Similar to naturally occurring peroxidases, DyPs are not optimized for industrial utilization owing to their inactivation induced by excess amounts of H2O2. -
Lysine and Novel Hydroxylysine Lipids in Soil Bacteria: Amino Acid Membrane Lipid Response to Temperature and Ph in Pseudopedobacter Saltans
Rowan University Rowan Digital Works School of Earth & Environment Faculty Scholarship School of Earth & Environment 6-1-2015 Lysine and novel hydroxylysine lipids in soil bacteria: amino acid membrane lipid response to temperature and pH in Pseudopedobacter saltans Elisha Moore Rowan University Ellen Hopmans W. Irene Rijpstra Irene Sanchez Andrea Laura Villanueva See next page for additional authors Follow this and additional works at: https://rdw.rowan.edu/see_facpub Part of the Environmental Microbiology and Microbial Ecology Commons Recommended Citation Moore, E.K., Hopmans, E., Rijpstra, W.I.C., Sanchez-Andrea, I., Villanueva, L., Wienk, H., ...& Sinninghe Damste, J. (2015). Lysine and novel hydroxylysine lipids in soil bacteria: amino acid membrane lipid response to temperature and pH in Pseudopedobacter saltans. Frontiers in Microbiology, Volume 6, Article 637. This Article is brought to you for free and open access by the School of Earth & Environment at Rowan Digital Works. It has been accepted for inclusion in School of Earth & Environment Faculty Scholarship by an authorized administrator of Rowan Digital Works. Authors Elisha Moore, Ellen Hopmans, W. Irene Rijpstra, Irene Sanchez Andrea, Laura Villanueva, Hans Wienk, Frans Schoutsen, Alfons Stams, and Jaap Sinninghe Damsté This article is available at Rowan Digital Works: https://rdw.rowan.edu/see_facpub/17 ORIGINAL RESEARCH published: 29 June 2015 doi: 10.3389/fmicb.2015.00637 Lysine and novel hydroxylysine lipids in soil bacteria: amino acid membrane lipid response to temperature and pH in Pseudopedobacter saltans Eli K. Moore 1*, Ellen C. Hopmans 1, W. Irene C. Rijpstra 1, Irene Sánchez-Andrea 2, Laura Villanueva 1, Hans Wienk 3, Frans Schoutsen 4, Alfons J. -
Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue (Skin/Bone/Cartilage/Aminoacid Analysis)
Proc. Nat. Acad. Sci. USA Vol. 69, No. 9, pp. 2594-2598, September 1972 Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue (skin/bone/cartilage/aminoacid analysis) DAVID R. EYRE AND MELVIN J. GLIMCHER* Department of Orthopedic Surgery, Harvard Medical School, Children's Hospital Medical Center, Boston, Massachusetts 02115 Communicated by Francis 0. Schmitt, July 3, 1972 ABSTRACT Reducible compounds that participate don, bone, and cartilage collagens (3-11). Each tissue reveals in crosslinking were analyzed in hydroxylysine-deficient a unique distribution of these reducible crosslinks that changes collagens of patients with a heritable disorder of connec- tive tissue. After treatment with [3H1sodium borohydride, as the tissue matures and ages (8, 10). new compounds, as well as a totally different pattern of Since connective tissues of patients with this disorder are tritiated compounds, were found in hydroxylysine-de- deficient in hydroxylysine, a crosslink precursor, it seemed ficient collagen from skin as compared with age-matched likely that the reducible crosslinks would either be absent or controls. The amount of desmosines detected indicated collagen cross- that more elastin was present in abnormal skin than in abnormal. Such a deficiency or abnormality in control skin. linking might be responsible for changes in the solubility Bone collagen, which was not as deficient in hydroxy- characteristics of the collagen (1), and for changes in the lysine as skin collagen, had the same compounds as normal structural properties of the tissues and the consequent skeletal bone collagen, but their relative proportions were altered, and connective tissue abnormalities. consistent with a deficiency of hydroxylysine, a precursor of the crosslinks. -
Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using Biological and Chemical Codes
molecules Article Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using Biological and Chemical Codes Piotr Minkiewicz * , Małgorzata Darewicz , Anna Iwaniak and Marta Turło Department of Food Biochemistry, University of Warmia and Mazury in Olsztyn, Plac Cieszy´nski1, 10-726 Olsztyn-Kortowo, Poland; [email protected] (M.D.); [email protected] (A.I.); [email protected] (M.T.) * Correspondence: [email protected]; Tel.: +48-89-523-3715 Abstract: Phosphorylation represents one of the most important modifications of amino acids, peptides, and proteins. By modifying the latter, it is useful in improving the functional properties of foods. Although all these substances are broadly annotated in internet databases, there is no unified code for their annotation. The present publication aims to describe a simple code for the annotation of phosphopeptide sequences. The proposed code describes the location of phosphate residues in amino acid side chains (including new rules of atom numbering in amino acids) and the diversity of phosphate residues (e.g., di- and triphosphate residues and phosphate amidation). This article also includes translating the proposed biological code into SMILES, being the most commonly used chemical code. Finally, it discusses possible errors associated with applying the proposed code and in the resulting SMILES representations of phosphopeptides. The proposed code can be extended to describe other modifications in the future. Keywords: amino acids; peptides; phosphorylation; phosphate groups; databases; code; bioinformatics; cheminformatics; SMILES Citation: Minkiewicz, P.; Darewicz, M.; Iwaniak, A.; Turło, M. Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using 1. Introduction Biological and Chemical Codes. -
Fatty Acid Metabolism Mediated by 12/15-Lipoxygenase Is a Novel Regulator of Hematopoietic Stem Cell Function and Myelopoiesis
University of Pennsylvania ScholarlyCommons Publicly Accessible Penn Dissertations Spring 2010 Fatty Acid Metabolism Mediated by 12/15-Lipoxygenase is a Novel Regulator of Hematopoietic Stem Cell Function and Myelopoiesis Michelle Kinder University of Pennsylvania, [email protected] Follow this and additional works at: https://repository.upenn.edu/edissertations Part of the Immunology and Infectious Disease Commons Recommended Citation Kinder, Michelle, "Fatty Acid Metabolism Mediated by 12/15-Lipoxygenase is a Novel Regulator of Hematopoietic Stem Cell Function and Myelopoiesis" (2010). Publicly Accessible Penn Dissertations. 88. https://repository.upenn.edu/edissertations/88 This paper is posted at ScholarlyCommons. https://repository.upenn.edu/edissertations/88 For more information, please contact [email protected]. Fatty Acid Metabolism Mediated by 12/15-Lipoxygenase is a Novel Regulator of Hematopoietic Stem Cell Function and Myelopoiesis Abstract Fatty acid metabolism governs critical cellular processes in multiple cell types. The goal of my dissertation was to investigate the intersection between fatty acid metabolism and hematopoiesis. Although fatty acid metabolism has been extensively studied in mature hematopoietic subsets during inflammation, in developing hematopoietic cells the role of fatty acid metabolism, in particular by 12/ 15-Lipoxygenase (12/15-LOX), was unknown. The observation that 12/15-LOX-deficient (Alox15) mice developed a myeloid leukemia instigated my studies since leukemias are often a consequence of dysregulated hematopoiesis. This observation lead to the central hypothesis of this dissertation which is that polyunsaturated fatty acid metabolism mediated by 12/15-LOX participates in hematopoietic development. Using genetic mouse models and in vitro and in vivo cell development assays, I found that 12/15-LOX indeed regulates multiple stages of hematopoiesis including the function of hematopoietic stem cells (HSC) and the differentiation of B cells, T cells, basophils, granulocytes and monocytes.