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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: 2-keto-3-deoxy-D-arabinonate dehydratase

Gene: kdaD Accession Number: G-10049 (MetaCyc)

Species: Sulfolobus solfataricus

Subunit composition of 2-keto-3-deoxy-D-arabinonate dehydratase = [KdaD]4
         2-keto-3-deoxy-D-arabinonate dehydratase subunit = KdaD

Summary:
The native relative molecular mass of purified, recombinant 2-keto-3-deoxy-D-arabinonate dehydratase expressed in Escherichia coli was determined by nanoflow electrospray ionization mass spectrometry [Brouns06].

The crystal structure of the recombinant enzyme was solved at 2.1 Å resolution. It was shown to have a homotetrameric subunit structure and is a member of the fumarylacetoacetate hydrolase (FAH) superfamily. Structures of the enzyme in complex with divalent metal ions and the substrate analog 2-oxobutanoate or the product 2,5-dioxopentanoate provided the basis for a proposed enzymatic mechanism [Brouns08].
The 2-keto-3-deoxy-D-arabinonate dehydratase subunit was annotated as hypothetical protein SSO3118.
Locus tag SSO3118. Annotated as hypothetical protein.

Map Position: [2,868,858 -> 2,869,754]

Molecular Weight of Polypeptide: 33.803 kD (from nucleotide sequence)

Molecular Weight of Multimer: 132.85 kD (experimental) [Brouns06]

Unification Links: Entrez-gene:1453140 , Protein Model Portal:Q97UA0 , SMR:Q97UA0 , String:273057.SSO3118 , UniProt:Q97UA0

Relationship Links: InterPro:IN-FAMILY:IPR002529 , InterPro:IN-FAMILY:IPR011234 , PDB:Structure:2Q18 , PDB:Structure:2Q19 , PDB:Structure:2Q1A , PDB:Structure:2Q1C , PDB:Structure:2Q1D , PDB:Structure:3BQB , Pfam:IN-FAMILY:PF01557

Gene-Reaction Schematic: ?

Credits:
Created 01-Jun-2007 by Fulcher CA , SRI International


Enzymatic reaction of: 2-keto-3-deoxy-D-arabinonate dehydratase

EC Number: 4.2.1.141

2-dehydro-3-deoxy-D-arabinonate <=> 2,5-dioxopentanoate + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of pentose and pentitol degradation , D-arabinose degradation III

Summary:
2-Keto-3-deoxy-D-arabinonate dehydratase was assayed in an indirect assay using D-arabinonate dehydratase and D-arabinonate as substrate. It was also assayed indirctly using D-arabinonate dehydratase, 2-keto-3-deoxy-D-arabinonate dehydratase, and 2,5-dioxopentanoate dehydrogenase, which formed α-ketoglutarate as a product [Brouns06].


References

Brouns06: Brouns SJ, Walther J, Snijders AP, van de Werken HJ, Willemen HL, Worm P, de Vos MG, Andersson A, Lundgren M, Mazon HF, van den Heuvel RH, Nilsson P, Salmon L, de Vos WM, Wright PC, Bernander R, van der Oost J (2006). "Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment." J Biol Chem 281(37);27378-88. PMID: 16849334

Brouns08: Brouns SJ, Barends TR, Worm P, Akerboom J, Turnbull AP, Salmon L, van der Oost J (2008). "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(2);357-71. PMID: 18448118


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc11.