InChI=1S/C5H10O5/c6-1-3(8)5(10)4(9)2-7/h3,5-8,10H,1-2H2/t3-,5-/m1/s1 |
ZAQJHHRNXZUBTE-NQXXGFSBSA-N |
OC[C@@H](O)[C@@H](O)C(=O)CO |
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
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View more via ChEBI Ontology
D-erythro-pent-2-ulose
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D-ribulose
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D-Arabinoketose
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KEGG COMPOUND
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D-Arabinulose
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KEGG COMPOUND
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D-erythro-2-Pentulose
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KEGG COMPOUND
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D-erythro-Pent-2-ulose
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ChemIDplus
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D-Riboketose
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KEGG COMPOUND
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D-Ribulose
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KEGG COMPOUND
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D-ribulose
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UniProt
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D-Rul
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JCBN
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1723050
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Reaxys Registry Number
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Reaxys
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488-84-6
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CAS Registry Number
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KEGG COMPOUND
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488-84-6
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CAS Registry Number
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ChemIDplus
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Sarwar MW, Saleem IB, Ali A, Abbas F (2013) insilico Characterization and Homology Modeling of Arabitol Dehydrogenase (ArDH) from Candida albican. Bioinformation 9, 952-957 [PubMed:24391356] [show Abstract]
BackgroundArabitol dehydrogenase (ArDH) is involved in the production of different sugar alcohols like arabitol, sorbitol, mannitol, erythritol and xylitol by using five carbon sugars as substrate. Arabinose, d-ribose, d-ribulose, xylose and d-xylulose are known substrate of this enzyme. ArDH is mainly produced by osmophilic fungi for the conversion of ribulose to arabitol under stress conditions. Recently this enzyme has been used by various industries for the production of pharmaceutically important sugar alcohols form cheap source than glucose. But the information at structure level as well as its binding energy analysis with different substrates was missing.ResultsThe present study was focused on sequence analysis, insilico characterization and substrate binding analysis of ArDH from a fungus specie candida albican. Sequence analysis and physicochemical properties showed that this protein is highly stable, negatively charged and having more hydrophilic regions, these properties made this enzyme to bind with number of five carbon sugars as substrate. The predicted 3D model will helpful for further structure based studies. Docking analysis provided free energies of binding of each substrate from a best pose as arabinose -9.8224calK/mol, dribose -11.3701Kcal/mol, d-ribulose -8.9230Kcal/mol, xylose -9.7007Kcal/mol and d-xylulose 9.7802Kcal/mol.ConclusionOur study provided insight information of structure and interactions of ArDH with its substrate. These results obtained from this study clearly indicate that d-ribose is best substrate for ArDH for the production of sugar alcohols. This information will be helpful for better usage of this enzyme for hyper-production of sugar alcohols by different industries. | Moon HJ, Tiwari MK, Singh R, Kang YC, Lee JK (2012) Molecular determinants of the cofactor specificity of ribitol dehydrogenase, a short-chain dehydrogenase/reductase. Applied and environmental microbiology 78, 3079-3086 [PubMed:22344653] [show Abstract] Ribitol dehydrogenase from Zymomonas mobilis (ZmRDH) catalyzes the conversion of ribitol to d-ribulose and concomitantly reduces NAD(P)(+) to NAD(P)H. A systematic approach involving an initial sequence alignment-based residue screening, followed by a homology model-based screening and site-directed mutagenesis of the screened residues, was used to study the molecular determinants of the cofactor specificity of ZmRDH. A homologous conserved amino acid, Ser156, in the substrate-binding pocket of the wild-type ZmRDH was identified as an important residue affecting the cofactor specificity of ZmRDH. Further insights into the function of the Ser156 residue were obtained by substituting it with other hydrophobic nonpolar or polar amino acids. Substituting Ser156 with the negatively charged amino acids (Asp and Glu) altered the cofactor specificity of ZmRDH toward NAD(+) (S156D, [k(cat)/K(m)(,NAD)]/[k(cat)/K(m)(,NADP)] = 10.9, where K(m)(,NAD) is the K(m) for NAD(+) and K(m)(,NADP) is the K(m) for NADP(+)). In contrast, the mutants containing positively charged amino acids (His, Lys, or Arg) at position 156 showed a higher efficiency with NADP(+) as the cofactor (S156H, [k(cat)/K(m)(,NAD)]/[k(cat)/K(m)(,NADP)] = 0.11). These data, in addition to those of molecular dynamics and isothermal titration calorimetry studies, suggest that the cofactor specificity of ZmRDH can be modulated by manipulating the amino acid residue at position 156. | LeBlanc DJ, Mortlock RP (1971) Metabolism of D-arabinose: a new pathway in Escherichia coli. Journal of bacteriology 106, 90-96 [PubMed:4928018] [show Abstract] Several growth characteristics of Escherichia coli K-12 suggest that growth on l-fucose results in the synthesis of all the enzymes necessary for growth on d-arabinose. Conversely, when a mutant of E. coli is grown on d-arabinose, all of the enzymes necessary for immediate growth on l-fucose are present. Three enzymes of the l-fucose pathway in E. coli, l-fucose isomerase, l-fuculokinase, and l-fuculose-l-phospháte aldolase possess activity on d-arabinose, d-ribulose, and d-ribulose-l-phosphate, respectively. The products of the aldolase, with d-ribulose-l-phosphate as substrate, are dihydroxyacetone phosphate and glycolaldehyde. l-Fucose, but not d-arabinose, is capable of inducing these activities in wild-type E. coli. In mutants capable of utilizing d-arabinose as sole source of carbon and energy, these activities are induced in the presence of d-arabinose and in the presence of l-fucose. Mutants unable to utilize l-fucose, selected from strains capable of growth on d-arabinose, are found to have lost the ability to grow on d-arabinose. Enzymatic analysis of cell-free extracts, prepared from cultures of these mutants, reveals that a deficiency in any of the l-fucose pathway enzymes results in the loss of ability to utilize d-arabinose. Thus, the pathway of d-arabinose catabolism in E. coli K-12 is believed to be: d-arabinose right harpoon over left harpoon d-ribulose --> d-ribulose-l-phosphate right harpoon over left harpoon dihydroxyacetone phosphate plus glycolaldehyde. Evidence is presented which suggests that the glycolaldehyde is further oxidized to glycolate. |
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