Enzymes
UniProtKB help_outline | 24,361 proteins |
Enzyme class help_outline |
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- Name help_outline 6-phospho-D-glucono-1,5-lactone Identifier CHEBI:57955 Charge -2 Formula C6H9O9P InChIKeyhelp_outline IJOJIVNDFQSGAB-SQOUGZDYSA-L SMILEShelp_outline O[C@H]1[C@H](O)[C@@H](COP([O-])([O-])=O)OC(=O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 6-phospho-D-gluconate Identifier CHEBI:58759 (Beilstein: 3912778) help_outline Charge -3 Formula C6H10O10P InChIKeyhelp_outline BIRSGZKFKXLSJQ-SQOUGZDYSA-K SMILEShelp_outline O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:12556 | RHEA:12557 | RHEA:12558 | RHEA:12559 | |
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Publications
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NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase.
Miclet E., Stoven V., Michels P.A., Opperdoes F.R., Lallemand J.Y., Duffieux F.
The pentose-phosphate pathway provides reductive power and nucleotide precursors to the cell through oxidative and nonoxidative branches, respectively. 6-Phosphogluconolactonase is the second enzyme of the oxidative branch and catalyzes the hydrolysis of 6-phosphogluconolactones, the products of g ... >> More
The pentose-phosphate pathway provides reductive power and nucleotide precursors to the cell through oxidative and nonoxidative branches, respectively. 6-Phosphogluconolactonase is the second enzyme of the oxidative branch and catalyzes the hydrolysis of 6-phosphogluconolactones, the products of glucose 6-phosphate oxidation by glucose-6-phosphate dehydrogenase. The role of 6-phosphogluconolactonase was still questionable, because 6-phosphogluconolactones were believed to undergo rapid spontaneous hydrolysis. In this work, nuclear magnetic resonance spectroscopy was used to characterize the chemical scheme and kinetic features of the oxidative branch. We show that 6-phosphogluconolactones have in fact a nonnegligible lifetime and are highly electrophilic compounds. The delta form (1-5) of the lactone is the only product of glucose 6-phosphate oxidation. Subsequently, it leads to the gamma form (1-4) by intramolecular rearrangement. However, only the delta form undergoes spontaneous hydrolysis, the gamma form being a "dead end" of this branch. The delta form is the only substrate for 6-phosphogluconolactonase. Therefore, 6-phosphogluconolactonase activity accelerates hydrolysis of the delta form, thus preventing its conversion into the gamma form. Furthermore, 6-phosphogluconolactonase guards against the accumulation of delta-6-phosphogluconolactone, which may be toxic through its reaction with endogenous cellular nucleophiles. Finally, the difference between activity of human, Trypanosoma brucei, and Plasmodium falciparum 6-phosphogluconolactonases is reported and discussed. << Less
J Biol Chem 276:34840-34846(2001) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Purification of 6-phosphogluconolactonase from rat liver and yeast; its separation from gluconolactonase.
KAWADA M., KAGAWA Y., TAKIGUCHI H., SHIMAZONO N.