The Enzyme Database

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EC 4.2.1.5     
Accepted name: arabinonate dehydratase
Reaction: D-arabinonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
For diagram of reaction, click here
Other name(s): D-arabinonate hydro-lyase
Systematic name: D-arabinonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-36-6
References:
1.  Palleroni, N.J. and Doudoroff, M. Characterization and properties of 2-keto-3-deoxy-D-arabonic acid. J. Biol. Chem. 223 (1956) 499–508. [PMID: 13376619]
[EC 4.2.1.5 created 1961]
 
 
EC 4.2.1.82     
Accepted name: xylonate dehydratase
Reaction: D-xylonate = 2-dehydro-3-deoxy-D-arabinonate + H2O
Glossary: 2-dehydro-3-deoxy-D-arabinonate = 2-dehydro-3-deoxy-D-xylonate = 3-deoxy-L-glycero-pent-2-ulonate
Other name(s): D-xylo-aldonate dehydratase; D-xylonate dehydratase; D-xylonate hydro-lyase
Systematic name: D-xylonate hydro-lyase (2-dehydro-3-deoxy-D-arabinonate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 84788-77-2
References:
1.  Dahms, A.S. and Donald, A. D-xylo-Aldonate dehydratase. Methods Enzymol. 90 (1982) 302–305. [PMID: 7154961]
2.  Donald, A., Sibley, D., Lyons, D.E. and Dahms, A.S. D-Galactonate dehydrase. Purification and properties. J. Biol. Chem. 254 (1979) 2132–2137. [PMID: 422572]
[EC 4.2.1.82 created 1986]
 
 
EC 4.2.1.141     
Accepted name: 2-dehydro-3-deoxy-D-arabinonate dehydratase
Reaction: 2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O
Glossary: 2-dehydro-3-deoxy-D-arabinonate = 2-dehydro-3-deoxy-D-xylonate = 3-deoxy-L-glycero-pent-2-ulonate
Systematic name: 2-dehydro-3-deoxy-D-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)
Comments: The enzyme participates in pentose oxidation pathways that convert pentose sugars to the tricarboxylic acid cycle intermediate 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brouns, S.J., Walther, J., Snijders, A.P., van de Werken, H.J., Willemen, H.L., Worm, P., de Vos, M.G., Andersson, A., Lundgren, M., Mazon, H.F., van den Heuvel, R.H., Nilsson, P., Salmon, L., de Vos, W.M., Wright, P.C., Bernander, R. and van der Oost, J. Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment. J. Biol. Chem. 281 (2006) 27378–27388. [DOI] [PMID: 16849334]
2.  Brouns, S.J., Barends, T.R., Worm, P., Akerboom, J., Turnbull, A.P., Salmon, L. and van der Oost, J. Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily. J. Mol. Biol. 379 (2008) 357–371. [DOI] [PMID: 18448118]
3.  Johnsen, U., Dambeck, M., Zaiss, H., Fuhrer, T., Soppa, J., Sauer, U. and Schonheit, P. D-Xylose degradation pathway in the halophilic archaeon Haloferax volcanii. J. Biol. Chem. 284 (2009) 27290–27303. [DOI] [PMID: 19584053]
[EC 4.2.1.141 created 2013]
 
 


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