MetaCyc Enzyme: 5-dehydro-4-deoxy-D-glucarate dehydratase

Gene: kdgD Accession Number: G-11995 (MetaCyc)

Species: Acinetobacter sp. ADP1

Subunit composition of 5-dehydro-4-deoxy-D-glucarate dehydratase = [KdgD]4
         5-dehydro-4-deoxyglucarate dehydratase subunit = KdgD

The enzyme from Acinetobacter sp. ADP1 (previously known as Acinetobacter baylyi ADP1) was reported to be a homotetramer based on gel filtration data, but the native apparent molecular mass was not given [Aghaie08].

Recombinant enzyme was overexpressed in Escherichia coli and purified [Aghaie08].
Note that [Aghaie08] provided a subunit apparent molecular mass of 55 kDa as determined by SDS-PAGE, along with a calculated molecular mass of 51.36 kDa. However, these numbers do not agree with the computed molecular mass of 32.624 kDa found for this entry in the UniProt link below dated 2004.

Map Position: [134,254 -> 135,165]

Molecular Weight of Polypeptide: 51.36 kD (from nucleotide sequence), 55.0 kD (experimental) [Aghaie08]

Unification Links: Entrez-gene:2879972, Protein Model Portal:Q6FFQ1, String:62977.ACIAD0130, UniProt:Q6FFQ1

Relationship Links: InterPro:IN-FAMILY:IPR002220, InterPro:IN-FAMILY:IPR013785, InterPro:IN-FAMILY:IPR017655, Panther:IN-FAMILY:PTHR12128, Pfam:IN-FAMILY:PF00701, Prints:IN-FAMILY:PR00146

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 26-Apr-2010 by Fulcher CA, SRI International

Enzymatic reaction of: 5-dehydro-4-deoxy-D-glucarate dehydratase

Inferred from experiment

Synonyms: 5-keto-4-deoxy-glucarate dehydratase, 5-dehydro-4-deoxyglucarate dehydratase, KDG dehydratase

EC Number:

5-dehydro-4-deoxy-D-glucarate + H+ → CO2 + 2,5-dioxopentanoate + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of microbial D-galacturonate and D-glucuronate degradation, D-glucarate degradation II, D-galactarate degradation II

A coupled assay was used with an excess of the α-ketoglutaric semialdehyde dehydrogenase, measuring the rate to formation of NADPH. The enzyme showed hyperbolic kinetics for the dehydration and decarboxylation of 5-dehydro-4-deoxy-D-glucarate [Aghaie08].

Kinetic Parameters:
Substrate Km (μM) Citations
5-dehydro-4-deoxy-D-glucarate 203.0 [Aghaie08]


Aghaie08: Aghaie A, Lechaplais C, Sirven P, Tricot S, Besnard-Gonnet M, Muselet D, de Berardinis V, Kreimeyer A, Gyapay G, Salanoubat M, Perret A (2008). "New insights into the alternative D-glucarate degradation pathway." J Biol Chem 283(23);15638-46. PMID: 18364348

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 Pathway Tools version 19.5 (software by SRI International) on Tue Dec 1, 2015, biocyc13.