In enzymology, a 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) is an enzyme that catalyzes the chemical reaction

ATP + 2-dehydro-3-deoxy-D-gluconate ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

Thus, the two substrates of this enzyme are ATP and 2-dehydro-3-deoxy-D-gluconate, whereas its two products are ADP and 6-phospho-2-dehydro-3-deoxy-D-gluconate.[1]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-3-deoxy-D-gluconate 6-phosphotransferase. Other names in common use include 2-keto-3-deoxygluconokinase, 2-keto-3-deoxy-D-gluconic acid kinase, 2-keto-3-deoxygluconokinase (phosphorylating), 2-keto-3-deoxygluconate kinase, and ketodeoxygluconokinase. This enzyme participates in pentose phosphate pathway and pentose and glucuronate interconversions.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WYE.

References

  1. ^ Cynkin MA, Ashwell G (June 1960). "Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli". The Journal of Biological Chemistry. 235 (6): 1576–9. doi:10.1016/S0021-9258(19)76843-4. PMID 13813474.


Allikas: http://en.wikipedia.org/wiki/2-dehydro-3-deoxygluconokinase
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