Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline GDP-D-glucose Identifier CHEBI:58127 Charge -2 Formula C16H23N5O16P2 InChIKeyhelp_outline MVMSCBBUIHUTGJ-ZQVROCHNSA-L SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2R)-3-phosphoglycerate Identifier CHEBI:58272 Charge -3 Formula C3H4O7P InChIKeyhelp_outline OSJPPGNTCRNQQC-UWTATZPHSA-K SMILEShelp_outline O[C@H](COP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 24 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2R)-2-O-(α-D-glucopyranosyl)-3-phospho-glycerate Identifier CHEBI:62600 Charge -3 Formula C9H14O12P InChIKeyhelp_outline RJDBNSZFZDWPFL-CECBSOHTSA-K SMILEShelp_outline OC[C@H]1O[C@H](O[C@H](COP([O-])([O-])=O)C([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 184 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 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:31315 | RHEA:31316 | RHEA:31317 | RHEA:31318 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The effect of carbonic anhydrase inhibition on the velocity of thrombin-stimulated platelet aggregation under physiological conditions.
Siffert W., Fox G., Gros G.
We have studied the effect of ethoxzolamide , a specific carbonic anhydrase inhibitor, on the velocity of thrombin-stimulated platelet aggregation. After preincubation of platelet rich plasma with 10(-6) M ethoxzolamide the velocity of platelet aggregation was reduced by about 40%. Between 10(-11) ... >> More
We have studied the effect of ethoxzolamide , a specific carbonic anhydrase inhibitor, on the velocity of thrombin-stimulated platelet aggregation. After preincubation of platelet rich plasma with 10(-6) M ethoxzolamide the velocity of platelet aggregation was reduced by about 40%. Between 10(-11) M and 10(-10)M ethoxzolamide was necessary to achieve a half-maximal diminution of the aggregation velocity. An identical maximal reduction of the velocity of aggregation as with ethoxzolamide could be achieved by a nearly complete removal of CO2 from the platelet rich plasma. These results suggest that the intracellular CO2 hydration-dehydration reaction is involved in the activation of human platelets by thrombin. It is possible that the cytosolic carbonic anhydrase of platelets provides a rapid source of the protons that are transferred across the plasma membrane during the activation process. << Less
Biochem Biophys Res Commun 121:266-270(1984) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Identification of the mycobacterial glucosyl-3-phosphoglycerate synthase.
Empadinhas N., Albuquerque L., Mendes V., Macedo-Ribeiro S., da Costa M.S.
Mycobacteria synthesize unique polysaccharides that regulate fatty acid synthesis, namely the methylglucose lipopolysaccharide (MGLP) and the methylmannose polysaccharide. Glucosyl-(1-->2)-glycerate is found at the reducing end of MGLP. The mycobacterial gene encoding a glucosyl-3-phosphoglycerate ... >> More
Mycobacteria synthesize unique polysaccharides that regulate fatty acid synthesis, namely the methylglucose lipopolysaccharide (MGLP) and the methylmannose polysaccharide. Glucosyl-(1-->2)-glycerate is found at the reducing end of MGLP. The mycobacterial gene encoding a glucosyl-3-phosphoglycerate synthase (GpgS), primarily found in actinobacteria and sharing very low amino acid identity with known homo-functional GpgSs, has been identified. This gene has been annotated as an inverting family 2 glycosyltransferase of unknown function. The gpgS genes from the fast-growing Mycobacterium smegmatis strain 1102 and from the slow-growing Mycobacterium bovis BCG in Escherichia coli were expressed, and the recombinant enzymes were purified and characterized. The substrates for optimal activity were UDP-glucose and d-3-phosphoglycerate but ADP-glucose was also an efficient donor. The enzymes had maximal activity around 45 degrees C, pH 8.0, and were strictly dependent on Mg(2+). In Mycobacterium tuberculosis H37Rv, the gene encoding GpgS (Rv1208) is identical to the homologue in Mycobacterium bovis BCG and was considered to be essential for growth. It is shown that these genes encode retaining family 81 glycosyltransferases regardless of the low amino acid identity with other known enzymes of this family. << Less
FEMS Microbiol. Lett. 280:195-202(2008) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.