InChI=1S/C12H24O17P2/c13-1-2(14)5(17)10(6(18)3(1)15)28-31(25,26)29-12-8(20)4(16)7(19)11(9(12)21)27-30(22,23)24/h1-21H,(H,25,26)(H2,22,23,24)/p-3/t1-,2-,3+,4-,5-,6-,7-,8+,9+,10-,11+,12-/m0/s1 |
ZFRNHZNPYSOZBU-MCUIPIIISA-K |
O[C@H]1[C@H](O)[C@H](O)[C@H](OP([O-])(=O)O[C@H]2[C@H](O)[C@@H](O)[C@H](O)[C@@H](OP([O-])([O-])=O)[C@H]2O)[C@@H](O)[C@@H]1O |
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Outgoing
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bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate(3−)
(CHEBI:62576)
is a
inositol phosphate oxoanion
(CHEBI:76301)
bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate(3−)
(CHEBI:62576)
is conjugate base of
bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate
(CHEBI:62574)
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Incoming
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bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate
(CHEBI:62574)
is conjugate acid of
bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate(3−)
(CHEBI:62576)
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(1R,2S,3R,4R,5S,6S)-2,3,4,5,6-pentahydroxycyclohexyl (1S,2R,3S,4S,5R,6R)-2,3,4,6-tetrahydroxy-5-(phosphonatooxy)cyclohexyl phosphate
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bis(1L-myo-inositol) 3,1'-phosphate 1-phosphate
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UniProt
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Rodrigues MV, Borges N, Henriques M, Lamosa P, Ventura R, Fernandes C, Empadinhas N, Maycock C, da Costa MS, Santos H (2007) Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. Journal of bacteriology 189, 5405-5412 [PubMed:17526717] [show Abstract] The pathway for the synthesis of di-myo-inositol-phosphate (DIP) was recently elucidated on the basis of the detection of the relevant activities in cell extracts of Archaeoglobus fulgidus and structural characterization of products by nuclear magnetic resonance (NMR) (N. Borges, L. G. Gonçalves, M. V. Rodrigues, F. Siopa, R. Ventura, C. Maycock, P. Lamosa, and H. Santos, J. Bacteriol. 188:8128-8135, 2006). Here, a genomic approach was used to identify the genes involved in the synthesis of DIP. Cloning and expression in Escherichia coli of the putative genes for CTP:l-myo-inositol-1-phosphate cytidylyltransferase and DIPP (di-myo-inositol-1,3'-phosphate-1'-phosphate, a phosphorylated form of DIP) synthase from several (hyper)thermophiles (A. fulgidus, Pyrococcus furiosus, Thermococcus kodakaraensis, Aquifex aeolicus, and Rubrobacter xylanophilus) confirmed the presence of those activities in the gene products. The DIPP synthase activity was part of a bifunctional enzyme that catalyzed the condensation of CTP and l-myo-inositol-1-phosphate into CDP-l-myo-inositol, as well as the synthesis of DIPP from CDP-l-myo-inositol and l-myo-inositol-1-phosphate. The cytidylyltransferase was absolutely specific for CTP and l-myo-inositol-1-P; the DIPP synthase domain used only l-myo-inositol-1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-l-myo-inositol and CDP-d-myo-inositol, were recognized as alcohol donors. Genome analysis showed homologous genes in all organisms known to accumulate DIP and for which genome sequences were available. In most cases, the two activities (l-myo-inositol-1-P cytidylyltransferase and DIPP synthase) were fused in a single gene product, but separate genes were predicted in Aeropyrum pernix, Thermotoga maritima, and Hyperthermus butylicus. Additionally, using l-myo-inositol-1-phosphate labeled on C-1 with carbon 13, the stereochemical configuration of all the metabolites involved in DIP synthesis was established by NMR analysis. The two inositol moieties in DIP had different stereochemical configurations, in contradiction of previous reports. The use of the designation di-myo-inositol-1,3'-phosphate is recommended to facilitate tracing individual carbon atoms through metabolic pathways. | Izui K, Matsuda Y, Kameshita I, Katsuki H, Woods AE (1983) Phosphoenolpyruvate carboxylase of Escherichia coli. Inhibition by various analogs and homologs of phosphoenolpyruvate. Journal of biochemistry 94, 1789-1795 [PubMed:6368527] [show Abstract] In an attempt to investigate the topography of the catalytic site of phosphoenolpyruvate (PEP) carboxylase [EC 4.1.1.31] of Escherichia coli, the inhibitor constants (Ki) for more than 20 compounds were determined with the reaction system containing dioxane, a non-physiological activator of the enzyme. The Ki values for the compounds lacking methylene-, carboxylate-, or phosphate groups were all more than 10-fold larger than the Km value for PEP, indicating the significant contribution of these groups to the binding of PEP with the enzyme. The Ki value for L-phospholactate (0.30 mM) was almost equal to the Km value for PEP (0.25 mM), whereas that for D-phospholactate (0.89 mM) was about 3-fold larger than the Km value. It was presumed that PEP binds with the enzyme on its si-side. Among 6 PEP homologs, the Ki values for phosphoenol alpha-ketobutyrate (0.024 mM) and phosphoenol alpha-ketovalerate (0.034 mM) were about one-tenth the Km value, indicating the presence of a hydrophobic pocket around the binding site of the methylene group of PEP, where the carboxylation reaction is supposed to occur. DL-Phosphomalate, a presumptive carboxylated substrate, was a weak inhibitor with a Ki value of 2.20 mM. |
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