エピメラーゼ
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/06/08 02:14:53」(JST)
[Wiki en表示]
Epimerases and racemases are isomerase enzymes that catalyze the inversion of stereochemistry in biological molecules.[1] Racemases catalyze the stereochemical inversion around the asymmetric carbon atom in a substrate having only one center of asymmetry. Epimerases catalyze the stereochemical inversion of the configuration about an asymmetric carbon atom in a substrate having more than one center of asymmetry, thus interconverting epimers.
Human epimerases include methylmalonyl-CoA epimerase, involved in the metabolic breakdown of the amino acids alanine, isoleucine, methionine and valine,[2] and UDP-glucose 4-epimerase, which is used in the final step of galactose metabolism - catalyzing the reversible conversion of UDP-galactose to UDP-glucose.
References
- ^ Tanner, ME. (2002). "Understanding nature's strategies for enzyme-catalyzed racemization and epimerization". Acc. Chem. Res. 35 (4): 237–246. doi:10.1021/ar000056y. PMID 11955052.
- ^ http://www.britannica.com/science/isomerase
External links
- http://medical-dictionary.thefreedictionary.com/racemase
- http://medical-dictionary.thefreedictionary.com/epimerase
- Entry Term Epimerases at the US National Library of Medicine Medical Subject Headings (MeSH)
Isomerases: Epimerase and racemases (EC 5.1)
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5.1.1: Amino acids |
- Amino-acid racemase: Phenylalanine racemase (ATP-hydrolysing)
- Serine racemase
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5.1.2: Hydroxy acids |
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5.1.3: Carbohydrates |
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5.1.99: Other |
- Methylmalonyl CoA epimerase
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UpToDate Contents
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English Journal
- Occurrence and subcellular distribution of the NAD(P)HX repair system in mammals.
- Marbaix AY1, Tyteca D2, Niehaus TD3, Hanson AD3, Linster CL4, Van Schaftingen E1.Author information 1*Welbio, de Duve Institute, Université Catholique de Louvain, Avenue Hippocrate 75, B-1200 Brussels, Belgium.2†Cell Unit, de Duve Institute, Université Catholique de Louvain, Avenue Hippocrate 75, B-1200 Brussels, Belgium.3§Horticultural Sciences Department, University of Florida, Gainesville, FL 32611, U.S.A.4‡Luxembourg Centre for Systems Biomedicine, University of Luxembourg, Campus Belval, House of Biomedicine, Avenue des Hauts-Fourneaux 7, L-4362 Esch-sur-Alzette, Luxembourg.AbstractHydration of NAD(P)H to NAD(P)HX, which inhibits several dehydrogenases, is corrected by an ATP-dependent dehydratase and an epimerase recently identified as the products of the vertebrate Carkd (carbohydrate kinase domain) and Aibp (apolipoprotein AI-binding protein) genes respectively. The purpose of the present study was to assess the presence of these enzymes in mammalian tissues and determine their subcellular localization. The Carkd gene encodes proteins with a predicted mitochondrial propeptide (mCARKD), a signal peptide (spCARKD) or neither of them (cCARKD). Confocal microscopy analysis of transfected CHO (Chinese-hamster ovary) cells indicated that cCARKD remains in the cytosol, whereas mCARKD and spCARKD are targeted to the mitochondria and the endoplasmic reticulum respectively. Unlike the other two forms, spCARKD is N-glycosylated, supporting its targeting to the endoplasmic reticulum. The Aibp gene encodes two different proteins, which we show to be targeted to the mitochondria (mAIBP) and the cytosol (cAIBP). Quantification of the NAD(P)HX dehydratase and epimerase activities in rat tissues, performed after partial purification, indicated that both enzymes are widely distributed, with total activities of ≈3-10 nmol/min per g of tissue. Liver fractionation by differential centrifugation confirmed the presence of the dehydratase and the epimerase in the cytosol and in mitochondria. These data support the notion that NAD(P)HX repair is extremely widespread.
- The Biochemical journal.Biochem J.2014 May 15;460(1):49-58. doi: 10.1042/BJ20131482.
- Hydration of NAD(P)H to NAD(P)HX, which inhibits several dehydrogenases, is corrected by an ATP-dependent dehydratase and an epimerase recently identified as the products of the vertebrate Carkd (carbohydrate kinase domain) and Aibp (apolipoprotein AI-binding protein) genes respectively. The purpose
- PMID 24611804
- Synthesis of Flavonoid O-Pentosides by Escherichia coli through Engineering of Nucleotide Sugar Pathways and Glycosyltransferase.
- Han SH1, Kim BG, Yoon JA, Chong Y, Ahn JH.Author information 1Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, South Korea.AbstractPlants produce two flavonoid O-pentoses, flavonoid O-xyloside and flavonoid O-arabinoside. However, analyzing their biological properties is difficult because flavonoids are not naturally produced in sufficient quantities. In this study, Escherichia coli was used to synthesize the plant-specific flavonoid O-pentosides quercetin 3-O-xyloside and quercetin 3-O-arabinoside. Two strategies were used. First, E. coli was engineered to express components of the biosynthetic pathways for UDP-xylose and UDP-arabinose. For UDP-xylose biosynthesis, two genes, UXS (UDP-xylose synthase) from Arabidopsis thaliana and ugd (UDP-glucose dehydrogenase) from E. coli, were overexpressed. In addition, the gene encoding ArnA (UDP-l-Ara4N formyltransferase/UDP-GlcA C-4″-decarboxylase), which competes with UXS for UDP-glucuronic acid, was deleted. For UDP-arabinose biosynthesis, UXE (UDP-xylose epimerase) was overexpressed. Next, we engineered UDP-dependent glycosyltransferases (UGTs) to ensure specificity for UDP-xylose and UDP-arabinose. The E. coli strains thus obtained synthesized approximately 160 mg/liter of quercetin 3-O-xyloside and quercetin 3-O-arabinoside.
- Applied and environmental microbiology.Appl Environ Microbiol.2014 May;80(9):2754-62. doi: 10.1128/AEM.03797-13. Epub 2014 Feb 21.
- Plants produce two flavonoid O-pentoses, flavonoid O-xyloside and flavonoid O-arabinoside. However, analyzing their biological properties is difficult because flavonoids are not naturally produced in sufficient quantities. In this study, Escherichia coli was used to synthesize the plant-specific fla
- PMID 24561591
- Liquid Chromatography-Tandem Mass Spectrometry Enzyme Assay for UDP-Galactose 4'-Epimerase: Use of Fragment Intensity Ratio in Differentiation of Structural Isomers.
- Li Y1, Huang X, Harmonay L, Liu Y, Kellogg MD, Fridovich-Keil JL, Berry GT.Author information 1The Manton Center for Orphan Disease Research, Division of Genetics, Department of Pediatrics.AbstractBACKGROUND: Distinction between asymptomatic and potentially clinically significant forms of galactosemia due to UDP-galactose 4'-epimerase (GALE) deficiency requires enzyme measurement in erythrocytes and other cells. We sought to develop a GALE assay using a novel liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based method.
- Clinical chemistry.Clin Chem.2014 May;60(5):783-90. doi: 10.1373/clinchem.2013.219931. Epub 2014 Feb 27.
- BACKGROUND: Distinction between asymptomatic and potentially clinically significant forms of galactosemia due to UDP-galactose 4'-epimerase (GALE) deficiency requires enzyme measurement in erythrocytes and other cells. We sought to develop a GALE assay using a novel liquid chromatography-tandem mass
- PMID 24578239
Japanese Journal
- Signature-tagged mutagenesis of Vibrio vulnificus
- , , , , , , , , , , ,
- Journal of Veterinary Medical Science advpub(0), 2015
- … Transposon-inserted genes in the 11 attenuated mutants were those for IMP dehydrogenase, UDP-N-acetylglucosamine-2-epimerase, aspartokinase, phosphoribosylformylglycinamidine cyclo-ligase, malate Na (+) symporter and hypothetical protein. …
- NAID 130004781124
- Identification and Characterization of an Arabidopsis Mutant with Altered Localization of NIP5;1, a Plasma Membrane Boric Acid Channel, Reveals the Requirement for D-Galactose in Endomembrane Organization (Special Focus Issue : Plant Endomembranes)
- Uehara Masataka,Wang Sheliang,Kamiya Takehiro [他]
- Plant and cell physiology 55(4), 704-714, 2014-04
- NAID 40020302018
- Colorimetric Quantification of β-(1→4)-Mannobiose and 4-O-β-D-Mannosyl-D-glucose
- Jaito Nongluck,Saburi Wataru,Muto Hirohiko [他]
- Journal of applied glycoscience 61(4), 117-119, 2014
- NAID 40020270854
Related Links
- epimerase [ĕ-pim´er-āse] an isomerase enzyme that catalyzes a change in asymmetric groups in substrates (epimers) that have more than one center of asymmetry. e·pim·er·ase (ĕpim'ĕr-ās), A class of enzymes catalyzing epimeric ...
- Epimerase deficiency galactosemia (GALE deficiency galactosemia) is a continuum comprising three forms: ... Infants with generalized epimerase deficiency galactosemia develop clinical findings on a regular milk diet ...
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★リンクテーブル★
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- 英
- epimerase
- 英
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- 関
- イソメラーゼ、ラセマーゼ
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ラセマーゼ、ラセミ化酵素
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- epimerase、racemase and epimerase
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- 英
- epimerase
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- エピメラーゼ
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ラセマーゼとエピメラーゼ
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- epimerase、racemase