|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 ]
Enzymatic reaction of: 5-dehydro-4-deoxy-D-glucarate dehydratase
Synonyms: 5-keto-4-deoxy-glucarate dehydratase, 5-dehydro-4-deoxyglucarate dehydratase, KDG dehydratase
EC Number: 188.8.131.52
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.
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].
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
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