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{{enzyme
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| Name = 2-dehydro-3-deoxygluconokinase
| EC_number = 2.7.1.45
| CAS_number = 9026-54-4
| IUBMB_EC_number = 2/7/1/45
| GO_code = 0008673
| image =  
| width =
| caption =
}}
In [[enzymology]], a '''2-dehydro-3-deoxygluconokinase''' ({{EC number|2.7.1.45}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]


:ATP + 2-dehydro-3-deoxy-D-gluconate <math>\rightleftharpoons</math> ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[2-dehydro-3-deoxy-D-gluconate]], whereas its two [[product (chemistry)|products]] are [[adenosine diphosphate|ADP]] and [[6-phospho-2-dehydro-3-deoxy-D-gluconate]].
 
This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing groups ([[phosphotransferase]]s) 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 [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1WYE}}.
 
==References==
{{reflist|1}}
* {{cite journal | author = CYNKIN MA, ASHWELL G | date = 1960 | title = Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli | journal = J. Biol. Chem. | volume = 235 | pages = 1576&ndash;9  | pmid = 13813474 }}
 
{{enzyme-stub}}
 
[[Category:EC 2.7.1]]
[[Category:Enzymes of known structure]]

Latest revision as of 00:48, 8 September 2014

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