Biochemistry Day 21
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Molecular Characterization of Galactokinase Deficiency In
J Hum Genet (1999) 44:377–382 © Jpn Soc Hum Genet and Springer-Verlag 1999377 ORIGINAL ARTICLE Minoru Asada · Yoshiyuki Okano · Takuji Imamura Itsujin Suyama · Yutaka Hase · Gen Isshiki Molecular characterization of galactokinase deficiency in Japanese patients Received: May 19, 1999 / Accepted: August 21, 1999 Abstract Galactokinase (GALK) deficiency is an autoso- Key words Galactosemia · Galactokinase (GALK) · Muta- mal recessive disorder, which causes cataract formation in tion · Genotype · Phenotype children not maintained on a lactose-free diet. We charac- terized the human GALK gene by screening a Japanese genomic DNA phage library, and found that several nucle- otides in the 59-untranslated region and introns 1, 2, and 5 in Introduction our GALK genomic analysis differed from published data. A 20-bp tandem repeat was found in three places in intron Galactokinase (GALK: McKUSICK 230200) is the first 5, which were considered insertion sequences. We identified enzyme in the Leloir pathway of galactose metabolism; it five novel mutations in seven unrelated Japanese patients catalyzes the phosphorylation of galactose to galactose- with GALK deficiency. There were three missense muta- 1-phosphate. GALK deficiency, first described in 1965 tions and two deletions. All three missense mutations (Gitzelmann 1965), is an autosomal recessive genetic disor- (R256W, T344M, and G349S) occurred at CpG dinucle- der with an incidence of 1/1,000,000 in Japan (Aoki and otides, and the T344M and G349S mutations occurred in Wada 1988) on newborn mass screening and an incidence of the conserved region. The three missense mutations led to a 1/1,000,000 in Caucasians (Segal and Berry 1995). -
Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB
Table S1. Kinase clones included in human kinase cDNA library for yeast two-hybrid screening Gene Symbol Gene Description ACVR1B activin A receptor, type IB ADCK2 aarF domain containing kinase 2 ADCK4 aarF domain containing kinase 4 AGK multiple substrate lipid kinase;MULK AK1 adenylate kinase 1 AK3 adenylate kinase 3 like 1 AK3L1 adenylate kinase 3 ALDH18A1 aldehyde dehydrogenase 18 family, member A1;ALDH18A1 ALK anaplastic lymphoma kinase (Ki-1) ALPK1 alpha-kinase 1 ALPK2 alpha-kinase 2 AMHR2 anti-Mullerian hormone receptor, type II ARAF v-raf murine sarcoma 3611 viral oncogene homolog 1 ARSG arylsulfatase G;ARSG AURKB aurora kinase B AURKC aurora kinase C BCKDK branched chain alpha-ketoacid dehydrogenase kinase BMPR1A bone morphogenetic protein receptor, type IA BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase) BRAF v-raf murine sarcoma viral oncogene homolog B1 BRD3 bromodomain containing 3 BRD4 bromodomain containing 4 BTK Bruton agammaglobulinemia tyrosine kinase BUB1 BUB1 budding uninhibited by benzimidazoles 1 homolog (yeast) BUB1B BUB1 budding uninhibited by benzimidazoles 1 homolog beta (yeast) C9orf98 chromosome 9 open reading frame 98;C9orf98 CABC1 chaperone, ABC1 activity of bc1 complex like (S. pombe) CALM1 calmodulin 1 (phosphorylase kinase, delta) CALM2 calmodulin 2 (phosphorylase kinase, delta) CALM3 calmodulin 3 (phosphorylase kinase, delta) CAMK1 calcium/calmodulin-dependent protein kinase I CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha CAMK2B calcium/calmodulin-dependent -
Construction and Enzymatic Characterization of E
1 Minimizing acetate formation in E. coli fermentations 2 Marjan De Mey*, Sofie De Maeseneire, Wim Soetaert and Erick Vandamme 3 Ghent University, Laboratory of Industrial Microbiology and Biocatalysis, Department of 4 Biochemical and Microbial Technology, Faculty of Bioscience Engineering, Coupure links 5 653, B-9000 Ghent, Belgium 6 7 * Correspondence address: Marjan De Mey 8 Laboratory of Industrial Microbiology and Biocatalysis 9 Department of Biochemical and Microbial Technology 10 Faculty of Bioscience Engineering 11 Ghent University 12 Coupure links 653 13 B-9000 Gent 14 Tel: +32-9-264-60-28 15 Fax: +32-9-264-62-31 16 [email protected] 17 Keywords: acetate reduction, Escherichia coli, metabolic engineering 1 18 Abstract 19 Escherichia coli remains the best established production organisms in industrial 20 biotechnology. However, during aerobic fermentation runs at high growth rates, considerable 21 amounts of acetate are accumulated as by-product. This by-product has negative effects on 22 growth and protein production. Over the last 20 years, substantial research efforts have been 23 spent to reduce acetate accumulation during aerobic growth of E. coli on glucose. From the 24 onset it was clear that this quest should not be a simple nor uncomplicated one. Simple 25 deletion of the acetate pathway, reduced the acetate accumulation, but instead other by- 26 products were formed. This minireview gives a clear outline of these research efforts and the 27 outcome of them, including bioprocess level approaches and genetic approaches. Recently, 28 the latter seems to have some promising results. 29 30 1 Introduction 31 Escherichia coli was the first and is still one of the most commonly used production 32 organisms in industrial biotechnology. -
Effects of Glucagon, Glycerol, and Glucagon Plus Glycerol On
Iowa State University Capstones, Theses and Graduate Theses and Dissertations Dissertations 2011 Effects of glucagon, glycerol, and glucagon plus glycerol on gluconeogenesis, lipogenesis, and lipolysis in periparturient Holstein cows Nimer Mehyar Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/etd Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Mehyar, Nimer, "Effects of glucagon, glycerol, and glucagon plus glycerol on gluconeogenesis, lipogenesis, and lipolysis in periparturient Holstein cows" (2011). Graduate Theses and Dissertations. 11923. https://lib.dr.iastate.edu/etd/11923 This Thesis is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Graduate Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Effects of glucagon, glycerol, and glucagon plus glycerol on gluconeogenesis, lipogenesis, and lipolysis in periparturient Holstein cows by Nimer Mehyar A thesis submitted to graduate faculty in partial fulfillment of the requirements for the degree of MASTER OF SCIENCE Major: Biochemistry Program of Study Committee: Donald C. Beitz, Major Professor Ted W. Huiatt Kenneth J. Koehler Iowa State University Ames, Iowa 2011 Copyright Nimer Mehyar, 2011. All rights reserved ii To My Mother To Ghada Ali, Sarah, and Hassan -
Galactokinase (B) Glucokinase (C) Galactose-1-Phosphate Uridyltransferase (D) UDP-Galactose 4- Epimerase Sol
1. Which of the following enzymes are not involved in galactose metabolism? (a) Galactokinase (b) Glucokinase (c) Galactose-1-Phosphate Uridyltransferase (d) UDP-Galactose 4- epimerase Sol. (b) Glucokinase. 2. Which of the following enzymes leads to a glycogen storage disease known as Tarui’s disease? (a) Glucokinase (b) Pyruvate Kinase (c) Phosphofructokinase (d) Phosphoglucomutase Sol. (c) Phosphofructokinase. 3. Which of the following enzymes is defective in galactosemia- a fatal genetic disorder in infants? (a) Glucokinase (b) Galactokinase (c) UDP-Galactose 4- epimerase (d) Galactose-1-Phosphate Uridyltransferase Sol. (d) Galactose-1-Phosphate Uridyltransferase. 4. Which of the following enzyme deficiency leads to hemolytic anaemia? (a) Glucokinase (b) Pyruvate Kinase (c) Phosphoglucomutase (d) Phosphofructokinase Sol. (b) Pyruvate Kinase. 5. Which of the following glucose transporters are important in fructose transport in the intestine? (a) GLUT5 (b) GLUT3 (c) GLUT4 (d) GLUT7 Sol. (a) GLUT5. 6. Which of the following is a tricarboxylic acid? (a) Acetic acid (b) Succinic acid (c) Oxaloacetic acid (d) Citric acid Sol.(d) Citric acid. 7. Which of the following enzymes plays an important role in tumour metabolism? (a) Glucokinase (b) Pyruvate Kinase M2 (c) Phosphoglucomutase (d) Phosphofructokinase Sol. (b) Pyruvate Kinase M2. 8. Which of the following metabolites negatively regulates pyruvate kinase? 1. (a) Citrate (b) Alanine (c) Acetyl CoA (d) Fructose-1,6-Bisphosphate Sol. (b) Alanine 9. The glycerol phosphate shuttle functions in___________. (a) Lipid catabolism (b) Triglyceride synthesis (c) Anaerobic glycolysis for the regeneration of NAD (d) Aerobic glycolysis to transport NADH equivalents resulting from glycolysis into mitochondria. Sol. (d) Aerobic glycolysis to transport NADH equivalents resulting from glycolysis into mitochondria. -
• Glycolysis • Gluconeogenesis • Glycogen Synthesis
Carbohydrate Metabolism! Wichit Suthammarak – Department of Biochemistry, Faculty of Medicine Siriraj Hospital – Aug 1st and 4th, 2014! • Glycolysis • Gluconeogenesis • Glycogen synthesis • Glycogenolysis • Pentose phosphate pathway • Metabolism of other hexoses Carbohydrate Digestion! Digestive enzymes! Polysaccharides/complex carbohydrates Salivary glands Amylase Pancreas Oligosaccharides/dextrins Dextrinase Membrane-bound Microvilli Brush border Maltose Sucrose Lactose Maltase Sucrase Lactase ‘Disaccharidase’ 2 glucose 1 glucose 1 glucose 1 fructose 1 galactose Lactose Intolerance! Cause & Pathophysiology! Normal lactose digestion Lactose intolerance Lactose Lactose Lactose Glucose Small Intestine Lactase lactase X Galactose Bacteria 1 glucose Large Fermentation 1 galactose Intestine gases, organic acid, Normal stools osmotically Lactase deficiency! active molecules • Primary lactase deficiency: อาการ! genetic defect, การสราง lactase ลด ลงเมออายมากขน, พบมากทสด! ปวดทอง, ถายเหลว, คลนไสอาเจยนภาย • Secondary lactase deficiency: หลงจากรบประทานอาหารทม lactose acquired/transient เชน small bowel เปนปรมาณมาก เชนนม! injury, gastroenteritis, inflammatory bowel disease! Absorption of Hexoses! Site: duodenum! Intestinal lumen Enterocytes Membrane Transporter! Blood SGLT1: sodium-glucose transporter Na+" Na+" •! Presents at the apical membrane ! of enterocytes! SGLT1 Glucose" Glucose" •! Co-transports Na+ and glucose/! Galactose" Galactose" galactose! GLUT2 Fructose" Fructose" GLUT5 GLUT5 •! Transports fructose from the ! intestinal lumen into enterocytes! -
THE AEROBIC (Air-Robic!) PATHWAYS
THE AEROBIC (air-robic!) PATHWAYS Watch this video on aerobic glycolysis: http://ow.ly/G5djv Watch this video on oxygen use: http://ow.ly/G5dmh Energy System 1 – The Aerobic Use of Glucose (Glycolysis) This energy system involves the breakdown of glucose (carbohydrate) to release energy in the presence of oxygen. The key to this energy system is that it uses OXYGEN to supply energy. Just like the anaerobic systems, there are many negatives and positives from using this pathway. Diagram 33 below summarises the key features of this energy system. When reading the details on the table keep in mind the differences between this and the previous systems that were looked at. In this way a perspective of their features can be appreciated and applied. Diagram 33: The Key Features of the Aerobic Glycolytic System Highlight 3 key features in the diagram that are important to the functioning of this system. 1: ------------------------------------------------------------------------------------------------------------------------------------------------------- 2: ------------------------------------------------------------------------------------------------------------------------------------------------------- 3: ------------------------------------------------------------------------------------------------------------------------------------------------------- Notes ---------------------------------------------------------------------------------------------------------------------------------------------------------- ---------------------------------------------------------------------------------------------------------------------------------------------------------- -
Amino Acid & Protein
Amino Acid & Protein DR. MD. MAHBUBUR RAHMAN MBBS, M. Phil . MSc.(Biotechnology) DEPT. OF BIOCHEMISTRY RAJSHAHI MEDICAL COLLEGE At the end of the session Student will be able to • Definition of amino acid, formation of peptide bond & its property • Biomedical importance of AA • Protein cycle At the end of the session Student will be able to • Classification of AA, • Isoelectric pH and 2D electrophoresis • Protein – definition, classification & structure, • purification of protein Biomedical Importance • Monomeric unit of Protein/ Polypeptide • Amino acid and their derivatives participate in diverse cellular function • Further discussed in functional classification Biomedical Importance Peptide performs prominent role in neuroendocrine system eg. Hormone , Neurotransmitter, Transporter Human lack of capability to synthesize 10 of the 20 common A-Acid (most of them α amino acid) Diversity of Protein function Enzyme and hormone regulate metabolism muscle movement by protein (contractile protein) Collagen fiber forms bone Ig fights against infectious Bacteria & viruses Bacitracin and gramicidin act a antibiotic Bleomycin act anticancer agent Amino Acid Are organic acid having both carboxyl group and amino group attach to same carbon atom. Peptide Bond In protein, amino acids are joined covalently By peptide Bond which are amide linkage Between the α-carboxyl group of one amino acid and the α- amino group of another Characteristic of peptide bond Net charge of amino acid at neutral pH • At physiologic pH all amino acid have a negatively charged group (- COO-) and positively charged group ( - NH3).----- is called amphoteric( ampholyte) Isoelectric pH The pH at which amino bears no net charge. The pH at which amino acid are electrically neutral that is the sum of positive charge equals the sum of negative charge Optical properties of amino acid α carbon of each amino acid are attached to four different group there fore amino acid have optical isomerism. -
Energy Metabolism: Gluconeogenesis and Oxidative Phosphorylation
International Journal for Innovation Education and Research www.ijier.net Vol:-8 No-09, 2020 Energy metabolism: gluconeogenesis and oxidative phosphorylation Luis Henrique Almeida Castro ([email protected]) PhD in the Health Sciences Graduate Program, Federal University of Grande Dourados Dourados, Mato Grosso do Sul – Brazil. Leandro Rachel Arguello Dom Bosco Catholic University Campo Grande, Mato Grosso do Sul – Brazil. Nelson Thiago Andrade Ferreira Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Geanlucas Mendes Monteiro Heath and Development in West Central Region Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Jessica Alves Ribeiro Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Juliana Vicente de Souza Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Sarita Baltuilhe dos Santos Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Fernanda Viana de Carvalho Moreto MSc., Nutrition, Food and Health Graduate Program, Federal University of Grande Dourados Dourados, Mato Grosso do Sul – Brazil. Ygor Thiago Cerqueira de Paula Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. International Educative Research Foundation and Publisher © 2020 pg. 359 International Journal for Innovation Education and Research ISSN 2411-2933 September 2020 Vanessa de Souza Ferraz Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. Tayla Borges Lino Motion Science Graduate Program, Federal University of Mato Grosso do Sul Campo Grande, Mato Grosso do Sul – Brazil. -
Articles Catalytic Cycling in Β-Phosphoglucomutase: a Kinetic
9404 Biochemistry 2005, 44, 9404-9416 Articles Catalytic Cycling in â-Phosphoglucomutase: A Kinetic and Structural Analysis†,‡ Guofeng Zhang, Jianying Dai, Liangbing Wang, and Debra Dunaway-Mariano* Department of Chemistry, UniVersity of New Mexico, Albuquerque, New Mexico 87131-0001 Lee W. Tremblay and Karen N. Allen* Department of Physiology and Biophysics, Boston UniVersity School of Medicine, Boston, Massachusetts 02118-2394 ReceiVed March 26, 2005; ReVised Manuscript ReceiVed May 18, 2005 ABSTRACT: Lactococcus lactis â-phosphoglucomutase (â-PGM) catalyzes the interconversion of â-D-glucose 1-phosphate (â-G1P) and â-D-glucose 6-phosphate (G6P), forming â-D-glucose 1,6-(bis)phosphate (â- G16P) as an intermediate. â-PGM conserves the core domain catalytic scaffold of the phosphatase branch of the HAD (haloalkanoic acid dehalogenase) enzyme superfamily, yet it has evolved to function as a mutase rather than as a phosphatase. This work was carried out to identify the structural basis underlying this diversification of function. In this paper, we examine â-PGM activation by the Mg2+ cofactor, â-PGM activation by Asp8 phosphorylation, and the role of cap domain closure in substrate discrimination. First, the 1.90 Å resolution X-ray crystal structure of the Mg2+-â-PGM complex is examined in the context of + + previously reported structures of the Mg2 -R-D-galactose-1-phosphate-â-PGM, Mg2 -phospho-â-PGM, and Mg2+-â-glucose-6-phosphate-1-phosphorane-â-PGM complexes to identify conformational changes that occur during catalytic turnover. The essential role of Asp8 in nucleophilic catalysis was confirmed by demonstrating that the D8A and D8E mutants are devoid of catalytic activity. -
Hereditary Galactokinase Deficiency J
Arch Dis Child: first published as 10.1136/adc.46.248.465 on 1 August 1971. Downloaded from Alrchives of Disease in Childhood, 1971, 46, 465. Hereditary Galactokinase Deficiency J. G. H. COOK, N. A. DON, and TREVOR P. MANN From the Royal Alexandra Hospital for Sick Children, Brighton, Sussex Cook, J. G. H., Don, N. A., and Mann, T. P. (1971). Archives of Disease in Childhood, 46, 465. Hereditary galactokinase deficiency. A baby with galactokinase deficiency, a recessive inborn error of galactose metabolism, is des- cribed. The case is exceptional in that there was no evidence of gypsy blood in the family concerned. The investigation of neonatal hyperbilirubinaemia led to the discovery of galactosuria. As noted by others, the paucity of presenting features makes early diagnosis difficult, and detection by biochemical screening seems desirable. Cataract formation, of early onset, appears to be the only severe persisting complication and may be due to the biosynthesis and accumulation of galactitol in the lens. Ophthalmic surgeons need to be aware of this enzyme defect, because with early diagnosis and dietary treatment these lens changes should be reversible. Galactokinase catalyses the conversion of galac- and galactose diabetes had been made in this tose to galactose-l-phosphate, the first of three patient (Fanconi, 1933). In adulthood he was steps in the pathway by which galactose is converted found to have glycosuria as well as galactosuria, and copyright. to glucose (Fig.). an unexpectedly high level of urinary galactitol was detected. He was of average intelligence, and his handicaps, apart from poor vision, appeared to be (1) Galactose Gackinase Galactose-I-phosphate due to neurofibromatosis. -
Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance Naoki Kumashiro,1,2 Sara A
ORIGINAL ARTICLE Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance Naoki Kumashiro,1,2 Sara A. Beddow,3 Daniel F. Vatner,2 Sachin K. Majumdar,2 Jennifer L. Cantley,1,2 Fitsum Guebre-Egziabher,2 Ioana Fat,2 Blas Guigni,2 Michael J. Jurczak,2 Andreas L. Birkenfeld,2 Mario Kahn,2 Bryce K. Perler,2 Michelle A. Puchowicz,4 Vara Prasad Manchem,5 Sanjay Bhanot,5 Christopher D. Still,6 Glenn S. Gerhard,6 Kitt Falk Petersen,2 Gary W. Cline,2 Gerald I. Shulman,1,2,7 and Varman T. Samuel2,3 – We measured the mRNA and protein expression of the key transcriptional factors and cofactors (8 12). Yet, despite gluconeogenic enzymes in human liver biopsy specimens and the high degree of transcription regulation for these found that only hepatic pyruvate carboxylase protein levels enzymes, the control they exert over gluconeogenic flux is related strongly with glycemia. We assessed the role of pyruvate relatively weak (13–16). We recently reported that hepatic carboxylase in regulating glucose and lipid metabolism in rats expression of PEPCK and G6PC mRNA was not related to through a loss-of-function approach using a specific antisense fasting hyperglycemia in two rodent models of type 2 di- oligonucleotide (ASO) to decrease expression predominantly in abetes and in patients with type 2 diabetes (17). Thus, we liver and adipose tissue. Pyruvate carboxylase ASO reduced hypothesized that other mechanisms must account for in- plasma glucose concentrations and the rate of endogenous glucose production in vivo. Interestingly, pyruvate carboxylase ASO also creased hepatic gluconeogenesis and fasting hyperglycemia reduced adiposity, plasma lipid concentrations, and hepatic in type 2 diabetes.