コリン脱水素酵素、コリンデヒドロゲナーゼ
WordNet
- a B-complex vitamin that is a constituent of lecithin; essential in the metabolism of fat
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/04/19 11:17:28」(JST)
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choline dehydrogenase |
Identifiers |
EC number |
1.1.99.1 |
CAS number |
9028-67-5 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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In enzymology, a choline dehydrogenase (EC 1.1.99.1) is an enzyme that catalyzes the chemical reaction
- choline + acceptor betaine aldehyde + reduced acceptor
Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products are betaine aldehyde and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is choline:acceptor 1-oxidoreductase. Other names in common use include choline oxidase, choline-cytochrome c reductase, choline:(acceptor) oxidoreductase, and choline:(acceptor) 1-oxidoreductase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, PQQ.
References
- Minoru Ameyama; Emiko Shinagawa; Kazunobu Matsushita; Koichi Takimoto; Koji Nakashima; Osao Adachi (1985). "Mammalian choline dehydrogenase is a quinoprotein". Agric. Biol. Chem. 49 (12): 3623–3626. doi:10.1271/bbb1961.49.3623.
- Ebisuzaki K, Williams JN (1955). "Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria". Biochem. J. 60 (4): 644–6. PMC 1216163. PMID 13249959.
- Gadda G, McAllister-Wilkins EE (2003). "Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata". Appl. Environ. Microbiol. 69 (4): 2126–32. doi:10.1128/AEM.69.4.2126-2132.2003. PMC 154813. PMID 12676692.
- Takabe T; Tanaka, Y; Aoki, K; Hibino, T; Jikuya, H; Takano, J; Takabe, T; Takabe, T (2003). "Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica". J. Biol. Chem. 278 (7): 4932–42. doi:10.1074/jbc.M210970200. PMID 12466265.
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
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1.1.1: NAD/NADP acceptor |
- 3-hydroxyacyl-CoA dehydrogenase
- 3-hydroxybutyryl-CoA dehydrogenase
- Alcohol dehydrogenase
- Aldo-keto reductase
- 1A1
- 1B1
- 1B10
- 1C1
- 1C3
- 1C4
- 7A2
- Aldose reductase
- Beta-Ketoacyl ACP reductase
- Carbohydrate dehydrogenases
- Carnitine dehydrogenase
- D-malate dehydrogenase (decarboxylating)
- DXP reductoisomerase
- Glucose-6-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- HMG-CoA reductase
- IMP dehydrogenase
- Isocitrate dehydrogenase
- Lactate dehydrogenase
- L-threonine dehydrogenase
- L-xylulose reductase
- Malate dehydrogenase
- Malate dehydrogenase (decarboxylating)
- Malate dehydrogenase (NADP+)
- Malate dehydrogenase (oxaloacetate-decarboxylating)
- Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
- Phosphogluconate dehydrogenase
- Sorbitol dehydrogenase
- Hydroxysteroid dehydrogenase: 3 Beta
- 11 Beta
- 17 Beta
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1.1.2: cytochrome acceptor |
- D-lactate dehydrogenase (cytochrome)
- D-lactate dehydrogenase (cytochrome c-553)
- Mannitol dehydrogenase (cytochrome)
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1.1.3: oxygen acceptor |
- Glucose oxidase
- L-gulonolactone oxidase
- Xanthine oxidase
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1.1.4: disulfide as acceptor |
- Vitamin K epoxide reductase
- Vitamin-K-epoxide reductase (warfarin-insensitive)
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1.1.5: quinone/similar acceptor |
- Malate dehydrogenase (quinone)
- Quinoprotein glucose dehydrogenase
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1.1.99: other acceptors |
- Choline dehydrogenase
- L2HGDH
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- Osmotic stress response in Acinetobacter baylyi: identification of a glycine-betaine biosynthesis pathway and regulation of osmoadaptive choline uptake and glycine-betaine synthesis through a choline-responsive BetI repressor.
- Scholz A1, Stahl J1, de Berardinis V2, Müller V1, Averhoff B1.
- Environmental microbiology reports.Environ Microbiol Rep.2016 Apr;8(2):316-22. doi: 10.1111/1758-2229.12382. Epub 2016 Feb 23.
- Acinetobacter baylyi, a ubiquitous soil bacterium, can cope with high salinity by uptake of choline as precursor of the compatible solute glycine betaine. Here, we report on the identification of a choline dehydrogenase (BetA) and a glycine betaine aldehyde dehydrogenase (BetB) mediating the oxidati
- PMID 26910138
- Transcription analysis of pyranose dehydrogenase from the basidiomycete Agaricus bisporus and characterization of the recombinantly expressed enzyme.
- Gonaus C1, Kittl R1, Sygmund C1, Haltrich D1, Peterbauer C2.
- Protein expression and purification.Protein Expr Purif.2016 Mar;119:36-44. doi: 10.1016/j.pep.2015.11.003. Epub 2015 Nov 23.
- Agaricus bisporus is a litter degrading basidiomycete commonly found in humic-rich environments. It is used as model organism and cultivated in large scale for food industry. Due to its ecological niche it produces a variety of enzymes for detoxification and degradation of humified plant litter. One
- PMID 26616098
- SIRT3 regulates α-SMA production through the succinate dehydrogenase-GPR91 pathway in hepatic stellate cells.
- Li YH1, Choi DH1, Lee EH2, Seo SR2, Lee S2, Cho EH3.
- The Journal of biological chemistry.J Biol Chem.2016 Feb 24. pii: jbc.M115.692244. [Epub ahead of print]
- Sirtuin 3 (SIRT3) is an NAD+-dependent protein deacetylase. Recent studies have shown that SIRT3 expression is decreased in nonalcoholic fatty liver disease (NAFLD). Moreover, SIRT3 is a key regulator of succinate dehydrogenase (SDH), which catalyzes the oxidation of succinate to fumarate. Increased
- PMID 26912655
Japanese Journal
- Retinol Status and Expression of Retinol-Related Proteins in Methionine-Choline Deficient Rats
- MIYAZAKI Hiroshi,TAKITANI Kimitaka,KOH Maki,INOUE Akiko,KISHI Kanta,TAMAI Hiroshi
- Journal of Nutritional Science and Vitaminology 60(2), 78-85, 2014
- … The purpose of this study was to evaluate the retinol status and expression of retinol-related proteins, including enzymes and binding proteins, in methionine-choline deficient (MCD) rats as a model of NAFLD. … We examined retinol levels in the plasma and liver and gene expression for β-carotene 15,15′-monooxygenase (BCMO), lecithIn: retinol acyltransferase (LRAT), aldehyde dehydrogenase 1A1 (ALDH1A1), ALDH1A2, and cellular retinol binding protein (CRBP)-I in MCD rats. …
- NAID 130004491369
- Tissue Localization of the Glycine Betaine Biosynthetic Enzymes in Barley Leaves
- Mitsuya Shiro,Kozaki Katsutoshi,Takabe Tetsuko
- Plant Production Science 16(2), 117-122, 2013
- … In barley, GB is produced by a two-step oxidation of choline in a cooperative way in the cytosol and peroxisomes. … In this study, we investigated the localization of two GB biosynthetic enzymes, choline monooxygenase (CMO) and betaine aldehyde dehydrogenase (BADH), in the tissues of barley plants (cv. …
- NAID 130004850071
- Clinical metabolomics using <SUP>1</SUP>H NMR spectral data in acute drug-induced liver injury
- KIM Ji Won,JO Haeran,KIM Siwon,SEO Jeong Ju,CHA Jaemin,LEE Hae Won,LIM Mi-Sun,SEONG Sook Jin,KIM Suhkmann,YOON Young-Ran,KIM Kyu-Bong
- 日本毒性学会学術年会 39.2(0), AP-15, 2012
- … All the subjects didn't show significant changes in alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), γ-glutamyl transpeptidase (γ-GTP), and lactate dehydrogenase (LDH) by APAP compared to before treatment. …
- NAID 130005009086
Related Links
- Biochemical Pharmacology, Vol. 30, No. 21, pp. 2993-3000, 1981. Printed in Great Britain. 0006-2952/81/212993-08 $02.00/0 1981 Pergamon Press Ltd. CHOLINE DEHYDROGENASE ASSAY, PROPERTIES AND ...
- Rabbit Polyclonal Anti-Choline dehydrogenase Antibody. Tested Applications: IHC, IHC-Paraffin. Tested Reactivity: Human. ... Species Human Tested Applications IHC, IHC-P Clonality Polyclonal Host Rabbit Gene CHDH Purity
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脱水素酵素 デヒドロゲナーゼ