D-キシルロース還元酵素、D-キシルロースレダクターゼ
WordNet
- the 4th letter of the Roman alphabet (同)d
- an enzyme that catalyses the biochemical reduction of some specified substance
PrepTutorEJDIC
- deuteriumの化学記号
- (おもに人称代名詞・固有名詞(人名),thereの後で)had, wouldの短縮形 / (疑問文でwhere,what,whenの後で)didの短縮形;Where'd he go?=Where did he go?
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/12/31 15:14:51」(JST)
[Wiki en表示]
| D-xylulose reductase |
| Identifiers |
| EC number |
1.1.1.9 |
| CAS number |
9028-16-4 |
| 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 D-xylulose reductase (EC 1.1.1.9) is an enzyme that catalyzes the chemical reaction
- xylitol + NAD+ D-xylulose + NADH + H+
Thus, the two substrates of this enzyme are xylitol and NAD+, whereas its 3 products are D-xylulose, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming). Other names in common use include NAD+-dependent xylitol dehydrogenase, xylitol dehydrogenase, erythritol dehydrogenase, 2,3-cis-polyol(DPN) dehydrogenase (C3-5), pentitol-DPN dehydrogenase, and xylitol-2-dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZEM.
References
- Chiang C, Knight SG (1960). "A new pathway of pentose metabolism". Biochem. Biophys. Res. Commun. 3 (5): 554–9. doi:10.1016/0006-291X(60)90174-1. PMID 13692998.
- Hickman J and Ashwell G (1959). "A sensitive and stereospecific enzymatic assay for xylulose". J. Biol. Chem. 234: 758–761.
- Jakoby WB, Fredericks J (1961). "Erythritol dehydrogenase from Aerobacter aerogenes". Biochim. Biophys. Acta 48: 26–32. doi:10.1016/0006-3002(61)90511-X. PMID 13789254.
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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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Proteins: enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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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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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Bioinformatics approaches for structural and functional analysis of proteins in secondary metabolism in Withania somnifera.
- Sanchita1, Singh S, Sharma A.
- Molecular biology reports.Mol Biol Rep.2014 Aug 2. [Epub ahead of print]
- Withania somnifera (Ashwagandha) is an affluent storehouse of large number of pharmacologically active secondary metabolites known as withanolides. These secondary metabolites are produced by withanolide biosynthetic pathway. Very less information is available on structural and functional aspects o
- PMID 25085038
- Increased accumulation of the cardio-cerebrovascular disease treatment drug tanshinone in Salvia miltiorrhiza hairy roots by the enzymes 3-hydroxy-3-methylglutaryl CoA reductase and 1-deoxy-D-xylulose 5-phosphate reductoisomerase.
- Shi M1, Luo X, Ju G, Yu X, Hao X, Huang Q, Xiao J, Cui L, Kai G.
- Functional & integrative genomics.Funct Integr Genomics.2014 Jun 10. [Epub ahead of print]
- Tanshinone is widely used for treatment of cardio-cerebrovascular diseases with increasing demand. Herein, key enzyme genes SmHMGR (3-hydroxy-3-methylglutaryl CoA reductase) and SmDXR (1-deoxy-D-xylulose 5-phosphate reductoisomerase) involved in the tanshinone biosynthetic pathway were introduced in
- PMID 24913677
- Effects of Streptomyces pactum Act12 on Salvia miltiorrhiza hairy root growth and tanshinone synthesis and its mechanisms.
- Yan Y1, Zhang S, Yang D, Zhang J, Liang Z.
- Applied biochemistry and biotechnology.Appl Biochem Biotechnol.2014 Jun;173(4):883-93. doi: 10.1007/s12010-014-0876-4. Epub 2014 Apr 15.
- The fermentation broth and mycelium pellet of Streptomyces pactum Act12 (Act12) may promote the accumulation of soluble sugar when added to Salvia miltiorrhiza hairy roots, increasing the accumulation level by as much as 23.20 % compared with the control; it may also inhibit the accumulation of sol
- PMID 24733528
Japanese Journal
- Cloning and Expression of a NAD^+-Dependent Xylitol Dehydrogenase Gene (xdhA) of Aspergillus oryzae(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Tran Lien Ha,Kitamoto Noriyuki,Kawai Keiichi [他],TAKAMIZAWA KAZUHIRO,SUZUKI TOHRU
- Journal of bioscience and bioengineering 97(6), 419-422, 2004-06-25
- XdhA, which encodes a xylitol dehydrogenase gene, was cloned from Aspergillus oryzae genomic DNA. It consists of 1214 bp structural region, which is interrupted by two introns, and encodes 358-amino-a …
- NAID 110002665322
- Cloning of the Xylitol Dehydrogenase Gene from Gluconobacter oxydans and Improved Production of Xylitol from D-Arabitol(Microbiology & Fermentation Technology)
- Sugiyama Masakazu,Suzuki Shun-ichi,Tonouchi Naoto [他],YOKOZEKI Kenzo
- Bioscience, biotechnology, and biochemistry 67(3), 584-591, 2003-03-23
- … The purified enzyme reduced D-xylulose to xylitol in the presence of NADH with an optimum pH of around 5.0. … The deduced amino acid sequence suggested that the enzyme belongs to the short-chain dehydrogenase/reductase family. …
- NAID 110002694102
- 42(P-1) 原核生物起源ジテルペンサイクラーゼ遺伝子に関する研究(ポスター発表の部)
- 大利 徹,濱野 吉十,伊藤 伸哉,葛山 智久,瀬戸 治男
- 天然有機化合物討論会講演要旨集 (42), 247-252, 2000-10-01
- … We have prepared a mutant lacking the 3-hydroxy-3methylglutaryl CoA (HMG-CoA) reductase activity from this strain, which uses both the mevalonate and nonmevalonate pathways for the formation of isopentenyl diphosphate, by screening terpentecin non-producing mutants. … The gene encoding HMG-CoA reductase (hmgr) was cloned and identified by complementation of the mutant, using a self-cloning system developed in this study for strain MF730-N6. …
- NAID 110006681944
Related Links
- In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that catalyzes the chemical reaction xylitol + NAD+ D-xylulose + NADH + H+ Thus, the two substrates of this enzyme are xylitol and NAD+, whereas its 3 products are ...
- Information on EC 1.1.1.9 - D-xylulose reductase BRENDA home login history all enzymes BRENDA home History Enzyme Nomenclature EC number Recommended Name Reaction Reaction Type Pathway Systematic Name ...
★リンクテーブル★
[★]
- 英
- D-xylulose reductase
- 関
- D-キシルロースレダクターゼ
[★]
- 英
- D-xylulose reductase
- 関
- D-キシルロース還元酵素
[★]
[★]
- (酵素)還元酵素、レダクターゼ、リダクターゼ
- 関
- dehydrogenase、oxidase、oxidoreductase、reducing enzyme