WordNet
- a salt of phosphoric acid (同)orthophosphate, inorganic_phosphate
- carbonated drink with fruit syrup and a little phosphoric acid
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- 〈U〉リン酸塩 / 《複数形で》リン酸肥料
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/09 16:42:17」(JST)
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- 1. ペルオキシソーム病 peroxisomal disorders
- 2. 幼児および小児における低血糖症の病因 etiology of hypoglycemia in infants and children
- 3. グリコーゲン代謝のその他の障害：GLUT2欠損症およびアルドラーゼA欠損症 other disorders of glycogen metabolism glut2 deficiency and aldolase a deficiency
- 4. 尋常性白斑 vitiligo
- 5. 日焼け sunburn
English Journal
- Structural and Functional Analysis of Fucose-Processing Enzymes from Streptococcus pneumoniae.
- Higgins MA1, Suits MD1, Marsters C1, Boraston AB2.Author information 1Department of Biochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, BC, V8W 3P6, Canada.2Department of Biochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, BC, V8W 3P6, Canada. Electronic address: boraston@uvic.ca.AbstractFucose metabolism pathways are present in many bacterial species and typically contain the central fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA). Fucose initially undergoes isomerization by FcsI producing fuculose, which is then phosphorylated by FcsK. FcsA cleaves the fuculose-1-phosphate product into lactaldehyde and dihydroxyacetone phosphate, which can be incorporated into central metabolism allowing the bacterium to use fucose as an energy source. Streptococcus pneumoniae has fucose-processing operons containing homologs of FcsI, FcsK, and FcsA; however, this bacterium appears unable to utilize fucose as an energy source. To investigate this contradiction, we performed biochemical and structural studies of the S. pneumoniae fucose-processing enzymes SpFcsI, SpFcsK, and SpFcsA. These enzymes are demonstrated to act in a sequential manner to ultimately produce dihydroxyacetone phosphate and have structural features entirely consistent with their observed biochemical activities. Analogous to the regulation of the Escherichia coli fucose utilization operon, fuculose-1-phosphate appears to act as an inducing molecule for activation of the S. pneumoniae fucose operon. Despite our evidence that S. pneumoniae appears to have the appropriate regulatory and biochemical machinery for fucose metabolism, we confirmed the inability of the S. pneumoniae TIGR4 strain to grow on fucose or on the H-disaccharide, which is the probable substrate of the transporter for the pathway. On the basis of these observations, we postulate that the S. pneumoniae fucose-processing pathway has a non-metabolic role in the interaction of this bacterium with its human host.
- Journal of molecular biology.J Mol Biol.2014 Apr 3;426(7):1469-82. doi: 10.1016/j.jmb.2013.12.006. Epub 2013 Dec 12.
- Fucose metabolism pathways are present in many bacterial species and typically contain the central fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA). Fucose initially undergoes isomerization by FcsI producing fuculose, which is then p
- PMID 24333485
- A comparative study on phosphotransferase activity of acid phosphatases from Raoultella planticola and Enterobacter aerogenes on nucleosides, sugars, and related compounds.
- Médici R1, Garaycoechea JI, Valino AL, Pereira CA, Lewkowicz ES, Iribarren AM.Author information 1Laboratorio de Biocatálisis y Biotransformaciones, Universidad Nacional de Quilmes, R.S. Peña 352. Bernal (1876), Buenos Aires, Argentina.AbstractNatural and modified nucleoside-5'-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activity. NSAP containing Enterobacter aerogenes and Raoultella planticola whole cells were evaluated in the phosphorylation of a wide range of nucleosides and nucleoside precursors using pyrophosphate as phosphate donor. To increase the productivity of the process, we developed two genetically modified strains of Escherichia coli which overexpressed NSAPs of E. aerogenes and R. planticola. These new recombinant microorganisms (E. coli BL21 pET22b-phoEa and E. coli BL21 pET22b-phoRp) showed higher activity than the corresponding wild-type strains. Reductions in the reaction times from 21 h to 60 min, from 4 h to 15 min, and from 24 h to 40 min in cases of dihydroxyacetone, inosine, and fludarabine, respectively, were obtained.
- Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2014 Apr;98(7):3013-22. doi: 10.1007/s00253-013-5194-1. Epub 2013 Aug 31.
- Natural and modified nucleoside-5'-monophosphates and their precursors are valuable compounds widely used in biochemical studies. Bacterial nonspecific acid phosphatases (NSAPs) are a group of enzymes involved in the hydrolysis of phosphoester bonds, and some of them exhibit phosphotransferase activ
- PMID 23995227
- The effect of CO2 on anaerobic succinate production by Corynebacterium glutamicum: carbon flux analysis by 13C-NMR.
- Rado X0161 DX1, Turner DL, Fonseca LL, Carvalho AL, Blombach B, Eikmanns B, Neves AR, Santos H.Author information 1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República - EAN, 2780-157 Oeiras, Portugal.AbstractCorynebacterium glutamicum wild type produces a mixture of lactic, succinic and acetic acid from glucose under oxygen deprivation. We investigated the effect of CO2 on the production of organic acids in a two-stage process: cells were grown aerobically in glucose and, subsequently, organic acid production by non-growing cells was studied under anaerobic conditions. The presence of CO2 caused an up to 3-fold increase in the succinate yield (1 mol per mol of glucose), and about 2-fold increase in acetate, both at the expense of L-lactate production; moreover, dihydroxyacetone formation was abolished. The redistribution of carbon fluxes in response to CO2 was estimated by using 13C-labelled glucose and 13C-NMR analysis of the labelling patterns in end-products. The flux analysis showed that 97% succinate was produced via the reductive part of the tricarboxylic acid cycle, the low activity of the oxidative branch being sufficient to provide the reducing equivalents needed for the redox balance. The flux via the pentose phosphate pathway was low (∼5%) regardless of the presence or absence of CO2. Moreover, there was a significant channelling of carbon to storage compounds (glycogen, trehalose), and concomitant catabolism of these reserves. The intracellular and extracellular pools of lactate and succinate were measured by in vivo-NMR and the stoichiometry (H+:organic acid) of the respective exporters was calculated. This study shows that it is feasible to take advantage of natural cellular regulation mechanisms to obtain high yields of succinate with C. glutamicum without genetic manipulation.
- Applied and environmental microbiology.Appl Environ Microbiol.2014 Mar 7. [Epub ahead of print]
- Corynebacterium glutamicum wild type produces a mixture of lactic, succinic and acetic acid from glucose under oxygen deprivation. We investigated the effect of CO2 on the production of organic acids in a two-stage process: cells were grown aerobically in glucose and, subsequently, organic acid prod
- PMID 24610842
Japanese Journal
- 1つの酵素が2つの反応を触媒するしくみ
- 西増 弘志,伏信 進矢,若木 高善
- 日本結晶学会誌 54(2), 113-118, 2012-04-30
- … Unlike ordinary enzymes, fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) catalyzes two distinct reactions : (1) the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate to FBP, and (2) the dephosphorylation of FBP to fructose-6-phosphate. …
- NAID 10030631990
- GPD1L Mutations and SCN5A Phosphorylation in Brugada Syndrome
- C. Makielski Jonathan
- Journal of Arrhythmia 27(Supplement), 15-15, 2011
- … The gene GPD1L encodes the glycerol phosphate dehydrogenase 1-like protein with homology to glycerol phosphate dehydrogenase (GPD1). … GPD1 catalyzes the reversible conversion of glycerol-3-phosphate (G3P) to dihydroxyacetone phosphate (DHAP). …
- NAID 130002129793
- アルドラーゼを用いた糖類合成の展開
- 杉山 雅一,GREENBERG William,WONG Chi-Huey
- 有機合成化学協会誌 : JOURNAL OF Synthetic Organic Chemistry JAPAN 66(6), 605-615, 2008-06-01
- … The practicality of formerly reported methods using dihydroxyacetone phosphate (DHAP) aldolase was limited by the high cost and instability of DHAP. … (1) Directed evolution of the L-rhamnulose 1-phosphate aldolase (RhaD) was employed to alter the donor substrate specificity of RhaD aldolase from DHAP to DHA. … (2) RhaD aldolase was found to accept non-phosphorylated dihydroxyacetone (DHA) as a donor substrate in the presence of borate. …
- NAID 10021175615
Related Links
- Dihydroxyacetone phosphateとは？goo Wikipedia (ウィキペディア) 。出典：Wikipedia（ウィキペディア）フリー百科事典。 Dihydroxyacetone phosphateとは - goo Wikipedia (ウィキペディア) gooトップ サイトマップ スタートページに設定 ...
- Dihydroxyacetone Phosphate a ketotriose monosaccharide monophosphate, a derivative of the trihydric alcohol glycerol, with phosphate groups linked by an ester bond to one of the alcohol groups. It is an intermediate product in the ...
Related Pictures
★リンクテーブル★
| リンク元 | 「フルクトース1,6-ビスリン酸」「ジヒドロキシアセトンリン酸」「DHAP」 |
| 関連記事 | 「phosphate」「dihydroxyacetone」 |
「フルクトース1,6-ビスリン酸」
- 英
- fructose 1,6-bisphosphate FBP
- 同
- フルクトース1,6-二リン酸 fructose 1,6-diphosphate
- 関
- [[]]
解糖系
「ジヒドロキシアセトンリン酸」
CH2-OH | C=0 | CH2-O-H2PO4
「DHAP」
[★] ジヒドロキシアセトンリン酸 dihydroxyacetone phosphate
「phosphate」
- n.
- 関
- inorganic phosphate、orthophosphate、orthophosphoric acid、phospho、phosphoester、phosphoric、phosphoric acid、phosphoric acid ester、phosphorus