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| Glucose 1-phosphate (also called Cori ester) is a glucose molecule with a phosphate group on the 1'-carbon. It can exist in either the α- or β-anomeric form. |
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Read full article at Wikipedia
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InChI=1S/C6H13O9P/c7- 1-2-3(8)4(9)5(10)6(14-2)15-16(11,12)13/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5-,6-/m1/s1 |
| HXXFSFRBOHSIMQ-VFUOTHLCSA-N |
| OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O |
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Chlamydomonas reinhardtii
(NCBI:txid3055)
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See:
PubMed
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fundamental metabolite
Any metabolite produced by all living cells.
(via D-glucopyranose 1-phosphate )
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View more via ChEBI Ontology
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α-D-glucopyranose 1-(dihydrogen phosphate)
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1-O-phosphono-α-D-glucopyranose
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ChEBI
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α-D-glucopyranosyl phosphate
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HMDB
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alpha-D-Glucose 1-phosphate
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KEGG COMPOUND
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alpha-D-Glucose-1-phosphate
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KEGG COMPOUND
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ALPHA-D-GLUCOSE-1-PHOSPHATE
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PDBeChem
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Cori ester
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KEGG COMPOUND
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D-Glucose 1-phosphate
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KEGG COMPOUND
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D-Glucose alpha-1-phosphate
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KEGG COMPOUND
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59-56-3
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CAS Registry Number
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KEGG COMPOUND
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59-56-3
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CAS Registry Number
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ChemIDplus
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87853
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Reaxys Registry Number
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Reaxys
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Rajashekhara E, Kitaoka M, Kim YK, Hayashi K (2002)
Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8.
Bioscience, biotechnology, and biochemistry 66, 2578-2586 [PubMed:12596851]
[show Abstract]
The cepA putative gene encoding a cellobiose phosphorylase of Thermotoga maritima MSB8 was cloned, expressed in Escherichia coli BL21-codonplus-RIL and characterized in detail. The maximal enzyme activity was observed at pH 6.2 and 80 degrees C. The energy of activation was 74 kJ/mol. The enzyme was stable for 30 min at 70 degrees C in the pH range of 6-8. The enzyme phosphorolyzed cellobiose in an random-ordered bi bi mechanism with the random binding of cellobiose and phosphate followed by the ordered release of D-glucose and alpha-D-glucose-1-phosphate. The Km for cellobiose and phosphate were 0.29 and 0.15 mM respectively, and the kcat was 5.4 s(-1). In the synthetic reaction, D-glucose, D-mannose, 2-deoxy-D-glucose, D-glucosamine, D-xylose, and 6-deoxy-D-glucose were found to act as glucosyl acceptors. Methyl-beta-D-glucoside also acted as a substrate for the enzyme and is reported here for the first time as a substrate for cellobiose phosphorylases. D-Xylose had the highest (40 s(-1)) kcat followed by 6-deoxy-D-glucose (17 s(-1)) and 2-deoxy-D-glucose (16 s(-1)). The natural substrate, D-glucose with the kcat of 8.0 s(-1) had the highest (1.1 x 10(4) M(-1) s(-1)) kcat/Km compared with other glucosyl acceptors. D-Glucose, a substrate of cellobiose phosphorylase, acted as a competitive inhibitor of the other substrate, alpha-D-glucose-1-phosphate, at higher concentrations. | Street IP, Withers SG (1995)
Probing the ionization state of substrate alpha-D-glucopyranosyl phosphate bound to glycogen phosphorylase b.
The Biochemical journal 308 ( Pt 3), 1017-1023 [PubMed:8948464]
[show Abstract]
The ionization state of the substrate alpha-D-glucopyranosyl phosphate bound at the active site of glycogen phosphorylase has been probed by a number of techniques. Values of Ki determined for a series of substrate analogue inhibitors in which the phosphate moiety bears differing charges suggest that the enzyme will bind both the monoanionic and dianionic substrates with approximately equal affinity. These results are strongly supported by 31P- and 19F-NMR studies of the bound substrate analogues alpha-D-glucopyranosyl 1-methylenephosphonate and 2-deoxy-2-fluoro-alpha-D-glucopyranosyl phosphate, which also suggest that the substrate can be bound in either ionization state. The pH-dependences of the inhibition constants K1 for these two analogues, which have substantially different phosphate pK2 values (7.3 and 5.9 respectively), are found to be essentially identical with the pH-dependence of K(m) values for the substrate, inhibition decreasing according to an apparent pKa value of 7.2. This again indicates that there is no specificity for monoanion or dianion binding and also reveals that binding is associated with the uptake of a proton. As the bound substrate is not protonated, this proton must be taken up by the proton. |
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