The Enzyme Database

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EC 4.1.2.55     
Accepted name: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
Reaction: (1) 2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
(2) 2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): 2-keto-3-deoxygluconate aldolase (ambiguous); KDGA (ambiguous)
Systematic name: 2-dehydro-3-deoxy-6-phospho-D-gluconate/2-dehydro-3-deoxy-6-phospho-D-galactonate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
Comments: In the archaeon Sulfolobus solfataricus the enzyme is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It utilizes 2-dehydro-3-deoxy-6-phosphate-D-gluconate and 2-dehydro-3-deoxy-6-phosphate-D-galactonate with similar catalytic efficiency. In vitro the enzyme can also catalyse the cleavage of the non-phosphorylated forms 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with much lower catalytic efficiency. cf. EC 4.1.2.21, 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Buchanan, C.L., Connaris, H., Danson, M.J., Reeve, C.D. and Hough, D.W. An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates. Biochem. J. 343 (1999) 563–570. [PMID: 10527934]
2.  Lamble, H.J., Theodossis, A., Milburn, C.C., Taylor, G.L., Bull, S.D., Hough, D.W. and Danson, M.J. Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus. FEBS Lett. 579 (2005) 6865–6869. [PMID: 16330030]
3.  Wolterink-van Loo, S., van Eerde, A., Siemerink, M.A., Akerboom, J., Dijkstra, B.W. and van der Oost, J. Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases. Biochem. J. 403 (2007) 421–430. [PMID: 17176250]
[EC 4.1.2.55 created 2014]
 
 


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