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Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways
biology Review Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways Antonin Ginguay 1,2, Luc Cynober 1,2,*, Emmanuel Curis 3,4,5,6 and Ioannis Nicolis 3,7 1 Clinical Chemistry, Cochin Hospital, GH HUPC, AP-HP, 75014 Paris, France; [email protected] 2 Laboratory of Biological Nutrition, EA 4466 PRETRAM, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France 3 Laboratoire de biomathématiques, plateau iB2, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France; [email protected] (E.C.); [email protected] (I.N.) 4 UMR 1144, INSERM, Université Paris Descartes, 75006 Paris, France 5 UMR 1144, Université Paris Descartes, 75006 Paris, France 6 Service de biostatistiques et d’informatique médicales, hôpital Saint-Louis, Assistance publique-hôpitaux de Paris, 75010 Paris, France 7 EA 4064 “Épidémiologie environnementale: Impact sanitaire des pollutions”, Faculté de Pharmacie, Université Paris Descartes, 75006 Paris, France * Correspondence: [email protected]; Tel.: +33-158-411-599 Academic Editors: Arthur J.L. Cooper and Thomas M. Jeitner Received: 26 October 2016; Accepted: 24 February 2017; Published: 6 March 2017 Abstract: Ornithine δ-aminotransferase (OAT, E.C. 2.6.1.13) catalyzes the transfer of the δ-amino group from ornithine (Orn) to α-ketoglutarate (aKG), yielding glutamate-5-semialdehyde and glutamate (Glu), and vice versa. In mammals, OAT is a mitochondrial enzyme, mainly located in the liver, intestine, brain, and kidney. In general, OAT serves to form glutamate from ornithine, with the notable exception of the intestine, where citrulline (Cit) or arginine (Arg) are end products. -
Adaptive Laboratory Evolution Enhances Methanol Tolerance and Conversion in Engineered Corynebacterium Glutamicum
ARTICLE https://doi.org/10.1038/s42003-020-0954-9 OPEN Adaptive laboratory evolution enhances methanol tolerance and conversion in engineered Corynebacterium glutamicum Yu Wang 1, Liwen Fan1,2, Philibert Tuyishime1, Jiao Liu1, Kun Zhang1,3, Ning Gao1,3, Zhihui Zhang1,3, ✉ ✉ 1234567890():,; Xiaomeng Ni1, Jinhui Feng1, Qianqian Yuan1, Hongwu Ma1, Ping Zheng1,2,3 , Jibin Sun1,3 & Yanhe Ma1 Synthetic methylotrophy has recently been intensively studied to achieve methanol-based biomanufacturing of fuels and chemicals. However, attempts to engineer platform micro- organisms to utilize methanol mainly focus on enzyme and pathway engineering. Herein, we enhanced methanol bioconversion of synthetic methylotrophs by improving cellular tolerance to methanol. A previously engineered methanol-dependent Corynebacterium glutamicum is subjected to adaptive laboratory evolution with elevated methanol content. Unexpectedly, the evolved strain not only tolerates higher concentrations of methanol but also shows improved growth and methanol utilization. Transcriptome analysis suggests increased methanol con- centrations rebalance methylotrophic metabolism by down-regulating glycolysis and up- regulating amino acid biosynthesis, oxidative phosphorylation, ribosome biosynthesis, and parts of TCA cycle. Mutations in the O-acetyl-L-homoserine sulfhydrylase Cgl0653 catalyzing formation of L-methionine analog from methanol and methanol-induced membrane-bound transporter Cgl0833 are proven crucial for methanol tolerance. This study demonstrates the importance of -
CYP2A6) by P53
Transcriptional Regulation of Human Stress Responsive Cytochrome P450 2A6 (CYP2A6) by p53 Hao Hu M.Biotech. (Biotechnology) 2012 The University of Queensland B.B.A. 2009 University of Electronic Science and Technology of China B.Sc. (Pharmacy) 2009 University of Electronic Science and Technology of China A thesis submitted for the degree of Doctor of Philosophy at The University of Queensland in 2016 School of Medicine ABSTRACT Human cytochrome P450 (CYP) 2A6 is highly expressed in the liver and the encoding gene is regulated by various stress activated transcription factors, such as the nuclear factor (erythroid-derived 2)-like 2 (Nrf-2). Unlike the other xenobiotic metabolising CYP enzymes (XMEs), CYP2A6 only plays a minor role in xenobiotic metabolism. The CYP2A6 is highly induced by multiple forms of cellular stress conditions, where XMEs expression is normally inhibited. Recent findings suggest that the CYP2A6 plays an important role in regulating BR homeostasis. A computer based sequence analysis on the 3 kb proximate CYP2A6 promoter revealed several putative binding sites for p53, a protein that mediates regulation of antioxidant and apoptosis pathways. In this study, the role of p53 in CYP2A6 gene regulation is demonstrated. The site closest to transcription start site (TSS) is highly homologous with the p53 consensus sequence. The p53 responsiveness of this site was confirmed by transfections with various stepwise deleted of CYP2A6-5’-Luc constructs containing the putative p53RE. Deletion of the putative p53RE resulted in a total abolishment of p53 responsiveness of CYP2A6 promoter. Specific binding of p53 to the putative p53RE was detected by electrophoresis mobility shift assay. -
Characterisation of Bilirubin Metabolic Pathway in Hepatic Mitochondria Siti Nur Fadzilah Muhsain M.Sc
Characterisation of Bilirubin Metabolic Pathway in Hepatic Mitochondria Siti Nur Fadzilah Muhsain M.Sc. (Medical Research) 2005 Universiti Sains Malaysia Postgrad. Dip. (Toxicology) 2003 University of Surrey B.Sc.(Biomed. Sc.) 2000 Universiti Putra Malaysia A thesis submitted for the degree of Doctor of Philosophy at The University of Queensland in 2014 School of Medicine ABSTRACT Bilirubin (BR), a toxic waste product of degraded haem, is a potent antioxidant at physiological concentrations. To achieve the maximum benefit of BR, its intracellular level needs to be carefully regulated. A system comprising of two enzymes, haem oxygenase-1 (HMOX1) and cytochrome P450 2A5 (CYP2A5) exists in the endoplasmic reticulum (ER), responsible for regulating BR homeostasis. This system is induced in response to oxidative stress. In this thesis, oxidative stress caused accumulation of these enzymes in mitochondria — major producers and targets of reactive oxygen species (ROS) — is demonstrated. To understand the significance of this intracellular targeting, properties of microsomal and mitochondrial BR metabolising enzymes were compared and the capacity of mitochondrial CYP2A5 to oxidise BR in response to oxidative stress is reported. Microsomes and mitochondrial fractions were isolated from liver homogenates of DBA/2J mice, administered with sub-toxic dose of pyrazole, an oxidant stressor. The purity of extracted organelles was determined by analysing the expressions and activities of their respective marker enzymes. HMOX1 and CYP2A5 were significantly increased in microsomes and even more so in mitochondria in response to pyrazole-induced oxidative stress. By contrast, the treatment did not increase either microsomes or mitochondrial Uridine-diphosphate-glucuronosyltransferase 1A1 (UGT1A1), the sole enzyme that catalyses BR elimination through glucuronidation. -
Aspirin Intervention for the Reduction of Colorectal Cancer Risk (ASPIRED): a Study Protocol for a Randomized Controlled Trial David A
Drew et al. Trials (2017) 18:50 DOI 10.1186/s13063-016-1744-z STUDYPROTOCOL Open Access ASPirin Intervention for the REDuction of colorectal cancer risk (ASPIRED): a study protocol for a randomized controlled trial David A. Drew1,2, Samantha M. Chin1,2, Katherine K. Gilpin1,2, Melanie Parziale1,2, Emily Pond1,2, Madeline M. Schuck1,2, Kathleen Stewart2, Meaghan Flagg3, Crystal A. Rawlings3, Vadim Backman4, Peter J. Carolan2, Daniel C. Chung2, Francis P. Colizzo III2, Matthew Freedman5, Manish Gala1,2, John J. Garber2, Curtis Huttenhower6, Dmitriy Kedrin2, Hamed Khalili1,2, Douglas S. Kwon3, Sanford D. Markowitz8, Ginger L. Milne9, Norman S. Nishioka2, James M. Richter2, Hemant K. Roy10, Kyle Staller1,2, Molin Wang6,7,11 and Andrew T. Chan1,2,5,11,12* Abstract Background: Although aspirin is recommended for the prevention of colorectal cancer, the specific individuals for whom the benefits outweigh the risks are not clearly defined. Moreover, the precise mechanisms by which aspirin reduces the risk of cancer are unclear. We recently launched the ASPirin Intervention for the REDuction of colorectal cancer risk (ASPIRED) trial to address these uncertainties. Methods/design: ASPIRED is a prospective, double-blind, multidose, placebo-controlled, biomarker clinical trial of aspirin use in individuals previously diagnosed with colorectal adenoma. Individuals (n = 180) will be randomized in a 1:1:1 ratio to low-dose (81 mg/day) or standard-dose (325 mg/day) aspirin or placebo. At two study visits, participants will provide lifestyle, dietary and biometric data in addition to urine, saliva and blood specimens. Stool, grossly normal colorectal mucosal biopsies and cytology brushings will be collected during a flexible sigmoidoscopy without bowel preparation. -
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ID: 19-0149 8 6 Q Pang et al. PHO patients with soft tissue 8:6 736–744 giant tumor caused by HPGD mutation RESEARCH The first case of primary hypertrophic osteoarthropathy with soft tissue giant tumors caused by HPGD loss-of-function mutation Qianqian Pang1,2, Yuping Xu1,3, Xuan Qi1, Yan Jiang1, Ou Wang1, Mei Li1, Xiaoping Xing1, Ling Qin2 and Weibo Xia1 1Department of Endocrinology, Key Laboratory of Endocrinology, Ministry of Health, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences, Beijing, China 2Musculoskeletal Research Laboratory and Bone Quality and Health Assessment Centre, Department of Orthopedics & Traumatology, The Chinese University of Hong Kong, Hong Kong SAR, Hong Kong 3Department of Endocrinology, The First Affiliated Hospital of Shanxi Medicalniversity, U Taiyuan, Shanxi, China Correspondence should be addressed to L Qin or W Xia: [email protected] or [email protected] Abstract Background: Primary hypertrophic osteoarthropathy (PHO) is a rare genetic multi-organic Key Words disease characterized by digital clubbing, periostosis and pachydermia. Two genes, f primary hypertrophic HPGD and SLCO2A1, which encodes 15-hydroxyprostaglandin dehydrogenase (15-PGDH) osteoarthropathy and prostaglandin transporter (PGT), respectively, have been reported to be related to f PHO PHO. Deficiency of aforementioned two genes leads to failure of prostaglandin E2 (PGE2) f HPGD mutation degradation and thereby elevated levels of PGE2. PGE2 plays an important role in f soft tumor tumorigenesis. Studies revealed a tumor suppressor activity of 15-PGDH in tumors, such f COX2 selective inhibitor treatment as lung, bladder and breast cancers. However, to date, no HPGD-mutated PHO patients presenting concomitant tumor has been documented. -
Phytic Acid (Phytate)/ Total Phosphorus
www.megazyme.com PHYTIC ACID (PHYTATE)/ TOTAL PHOSPHORUS Measured as phosphorus released by phytase and alkaline phosphatase ASSAY PROCEDURE K-PHYT 05/19 (50 Assays per Kit) © Megazyme 2019 INTRODUCTION: Phytic acid (phytate; myo-inositol 1,2,3,4,5,6-hexakisphosphate) is the primary source of inositol and storage phosphorus in plant seeds contributing ~ 70% of total phosphorus. The abundance of phytic acid in cereal grains is a concern in the foods and animal feeds industries because the phosphorus in this form is unavailable to monogastric animals due to a lack of endogenous phytases; enzymes specific for the dephosphorylation of phytic acid. In addition, the strong chelating characteristic of phytic acid reduces the bioavailability of other essential dietary nutrients such as minerals (e.g. Ca2+, Zn2+, Mg2+, Mn2+, Fe2+/3+), proteins and amino acids.2 High phytic acid content feeds are generally supplemented with inorganic phosphate, however this causes increased faecal phosphate levels and subsequent eutrophication of waterways. Alternatively, supplementation with commercial phytases is becoming increasingly popular and reduces the requirement for inorganic phosphate supplementation as well as the associated environmental issues. Currently, there is no commercially available, simple, quantitative method for phytic acid and, while such measurement is relatively complex, the generally accepted AOAC Method 986.11 has limitations.3 For each individual analysis the method requires cumbersome anion-exchange purification and a major inherent assumption here is that only phytic acid is purified. While this assumption is viable for non-processed grains for which phytic acid comprises at least 97% of total inositol phosphates, it is not viable for processed foods and feeds which can contain higher levels of some lower myo-inositol phosphate forms (i.e. -
|I|||||IIIHIII US005541.108A United States Patent (19) 11 Patent Number: 5,541,108 Fujiwara Et Al
|I|||||IIIHIII US005541.108A United States Patent (19) 11 Patent Number: 5,541,108 Fujiwara et al. (45) Date of Patent: Jul. 30, 1996 54 GLUCONOBACTER OXYDANS STRAINS 5,082,785 l/1992. Manning et al. .................. 435/252.32 75 Inventors: Akiko Fujiwara, Kamakura; Teruhide FOREIGN PATENT DOCUMENTS Sugisawa; Masako Shinjoh, both of 994119 9/1963 United Kingdom................... 435/138 Yokohama; Yutaka Setoguchi; Tatsuo Hoshino, both of Kamakura, all of OTHER PUBLICATIONS Japan Stanbury et al. Principles of fermentation Technology, 1984, Pergamon Press. 73 Assignee: Hoffmann-La Roche Inc., Nutley, N.J. ATCC Catalogue of Bacteria, 1989, p. 106. Tsukada et al, Biotechnology and Bioengineering, vol 14, 21 Appl. No. 266,998 1972 pp. 799-810, John Wiley & Sons, Inc. Makover, et al., Biotechnology and Bioengineering XVII, 22 Filed: Jun. 28, 1994 pp. 1485-1514 (1975). Related U.S. Application Data Isono, et al. Agr. Biol. Chem, 35 No. 4 pp. 424–431 (1968). Okazaki, et al, Agr. Biol. Chem 32 No. 10 pp. 1250-1255 63 Continuation of Ser. No. 183,924, Jan. 18, 1994, abandoned, (1968). which is a continuation of Ser. No. 16,478, Feb. 10, 1993, Martin etal, Eur. S. Appl. Microbiology3, pp. 91-95 (1976). abandoned, which is a continuation of Ser. No. 517,972, Apr. Acta Microbologica Sinica 20 (3):246-251 (1980) (Abstract 30, 1990, abandoned, which is a continuation of Ser. No. only). 899,586, Aug. 25, 1986, abandoned. Acta Microbiologica Sinica 21 (2): 185-191- (1981) 30 Foreign Application Priority Data (Abstract only). Aug. 28, 1985 GB United Kingdom ................... 852359 Primary Examiner Irene Marx Jul. -
Effect of Ph and Temperature on the Activity of Phytase Products Used In
Brazilian Journal of Poultry Science Revista Brasileira de Ciência Avícola Effect of ph and Temperature on the Activity of ISSN 1516-635X Jul - Sept 2012/ v.14 / n.3 / 159-232 Phytase Products Used in Broiler Nutrition Author(s) ABSTRACT Naves L de P1 Corrêa AD2 The activity of three commercial microbial phytase (Aspergillus Bertechini AG3 oryzae, A. niger, and Saccharomyces cerevisae) products used in broiler Gomide EM4 Santos CD dos2 nutrition was determined at different pH (2.0 to 9.0) and temperature (20 to 90°C) values. Enzymatic activity was determined according to the reaction of the phytase with its substrate (sodium phytate), in four replicates, and was expressed in units of phytase activity (FTU). A. oryzae phytase exhibited optimal activity at pH 4.0 and 40°C, but 1Graduate student in Monogastric Nutrition of its absolute activity was the lowest of the three phytases evaluated. the Animal Science Department − Federal A. niger phytase exhibited maximal activity close to pH 5.0 and 45oC, University of Lavras (UFLA). whereas S. cerevisae phytase presented its highest activity at pH close to 2Professor of the Chemistry Department/ UFLA. 4.5 and temperatures ranging between 50 and 60°C. It was concluded 3Professor of the Animal Science Department/ that A. niger and S. cerevisae phytase products exhibited the highest UFLA. absolute activities in vitro at pH and temperature values (pH lower than 4Ph. D. student in Monogastric Nutrition of o the Animal Science Department/UFLA. 5.0 and 41 C) corresponding to the ideal physiological conditions of broilers, which would theoretically allow high hydrolysis rate of the phytate contained in the feed. -
Peraturan Badan Pengawas Obat Dan Makanan Nomor 28 Tahun 2019 Tentang Bahan Penolong Dalam Pengolahan Pangan
BADAN PENGAWAS OBAT DAN MAKANAN REPUBLIK INDONESIA PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN NOMOR 28 TAHUN 2019 TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN DENGAN RAHMAT TUHAN YANG MAHA ESA KEPALA BADAN PENGAWAS OBAT DAN MAKANAN, Menimbang : a. bahwa masyarakat perlu dilindungi dari penggunaan bahan penolong yang tidak memenuhi persyaratan kesehatan; b. bahwa pengaturan terhadap Bahan Penolong dalam Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 10 Tahun 2016 tentang Penggunaan Bahan Penolong Golongan Enzim dan Golongan Penjerap Enzim dalam Pengolahan Pangan dan Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 7 Tahun 2015 tentang Penggunaan Amonium Sulfat sebagai Bahan Penolong dalam Proses Pengolahan Nata de Coco sudah tidak sesuai dengan kebutuhan hukum serta perkembangan ilmu pengetahuan dan teknologi sehingga perlu diganti; c. bahwa berdasarkan pertimbangan sebagaimana dimaksud dalam huruf a dan huruf b, perlu menetapkan Peraturan Badan Pengawas Obat dan Makanan tentang Bahan Penolong dalam Pengolahan Pangan; -2- Mengingat : 1. Undang-Undang Nomor 18 Tahun 2012 tentang Pangan (Lembaran Negara Republik Indonesia Tahun 2012 Nomor 227, Tambahan Lembaran Negara Republik Indonesia Nomor 5360); 2. Peraturan Pemerintah Nomor 28 Tahun 2004 tentang Keamanan, Mutu dan Gizi Pangan (Lembaran Negara Republik Indonesia Tahun 2004 Nomor 107, Tambahan Lembaran Negara Republik Indonesia Nomor 4424); 3. Peraturan Presiden Nomor 80 Tahun 2017 tentang Badan Pengawas Obat dan Makanan (Lembaran Negara Republik Indonesia Tahun 2017 Nomor 180); 4. Peraturan Badan Pengawas Obat dan Makanan Nomor 12 Tahun 2018 tentang Organisasi dan Tata Kerja Unit Pelaksana Teknis di Lingkungan Badan Pengawas Obat dan Makanan (Berita Negara Republik Indonesia Tahun 2018 Nomor 784); MEMUTUSKAN: Menetapkan : PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN. -
Dissertation
Dissertation Submitted to the Combined Faculties for the Natural Sciences and for Mathematics of the Ruperto-Carola University of Heidelberg, Germany for the Degree of Doctor of Natural Sciences Presented by Ann-Cathrin Hofer (M.Sc.) Born in Heidelberg, Germany Oral Examination: 12th of September 2016 Regulatory T cells protect the neonatal liver and secure the hepatic circadian rhythm Referees 1st Referee: Prof. Dr. Peter Angel 2nd Referee: Dr. Markus Feuerer This dissertation was performed and written during the period from November 2012 to May 2016 in the German Cancer Research Center (DKFZ) under the supervision of Prof. Dr. Peter Angel and direct supervision of Dr. Markus Feuerer. The dissertation was submitted to the Combined Faculties for the Natural Sciences and for Mathematics of the Ruperto-Carola University of Heidelberg, Germany in June 2016. German Cancer Research Center (DKFZ) Immune Tolerance (D100) Im Neuenheimer Feld 280 69120 Heidelberg, Germany I II Confirmation Hereby, I confirm that I have written this thesis independently, using only the results of my investigation unless otherwise stated. Furthermore, I declare that I have not submitted this thesis for a degree to any other academic or similar institution. Parts of this dissertation have been submitted for publishing: Regulatory T cells protect the liver early in life and safeguard the hepatic circadian rhythm Ann-Cathrin Hofer, Thomas Hielscher, David M. Richards, Michael Delacher, Ulrike Träger, Sophia Föhr, Artyom Vlasov, Marvin Wäsch, Marieke Esser, Annette Kopp-Schneider, Achim Breiling, Frank Lyko, Ursula Klingmüller, Peter Angel, Jakub Abramson, Jeroen Krijgsveld & Markus Feuerer Parts of the experiments in this dissertation were performed in collaboration with other research groups as follows: CG methylation analysis with the 454 pyrosequencing technology: Division of Epigenetics, DKFZ, Heidelberg Dr. -
Novel Amine Dehydrogenase from Leucine Dehydrogenase 19
DEVELOPMENT OF AN AMINE DEHYDROGENASE A Dissertation Presented to The Academic Faculty by Michael J. Abrahamson In Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the School of Chemical and Biomolecular Engineering Georgia Institute of Technology December 2012 DEVELOPMENT OF AN AMINE DEHYDROGENASE Approved by: Dr. Andreas S. Bommarius, Advisor Dr. Jeffrey Skolnick School of Chemical & Biomolecular School of Biology Engineering Georgia Institute of Technology Georgia Institute of Technology Dr. Christopher W. Jones Dr. John W. Wong School of Chemical & Biomolecular Biocatalysis Center of Emphasis Engineering Chemical Research & Development Georgia Institute of Technology Pfizer Global Research & Development Dr. Yoshiaki Kawajiri School of Chemical & Biomolecular Engineering Georgia Institute of Technology Date Approved: August 13, 2012 To my parents, Joseph & Deborah ACKNOWLEDGEMENTS First and foremost, I would like to thank my parents Joseph and Deborah. Your guidance and unconditional support has been invaluable to my success throughout college. The encouragement from my entire family has been so helpful throughout graduate school. I would also like to thank my advisor, Prof. Andreas Bommarius for his direction, instruction, and patience over the last five years. Your input and optimism has kept me ‘plowing ahead’ and has been instrumental in my scientific development. I would like to thank my committee members; Prof. Christopher Jones, Prof. Yoshiaki Kawajiri, Prof. Jeffrey Skolnick, and Dr. John W. Wong. Thank you all for your time, encouragement, and support. All of the members of the Bommarius lab, past and present, have made my graduate career not only productive, but enjoyable. We have shared many great and unforgettable moments.