|Gene:||gudD||Accession Number: G-11994 (MetaCyc)|
Species: Acinetobacter sp. ADP1
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].
The crystal structure of D-glucarate dehydratase from Pseudomonas putida has been determined [Gulick98].
Note that [Aghaie08] provided a subunit apparent molecular mass of 38 kDa as determined by SDS-PAGE, along with a calculated molecular mass of 34.96 kDa. However, these numbers do not agree with the computed molecular mass of 49.027 kDa found for this entry in the UniProt link below, dated 2004.
|Map Position: [132,209 -> 133,543]|
Molecular Weight of Polypeptide: 34.96 kD (from nucleotide sequence), 38.0 kD (experimental) [Aghaie08 ]
Enzymatic reaction of: D-glucarate dehydratase
EC Number: 220.127.116.11
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.
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
Gulick98: Gulick AM, Palmer DR, Babbitt PC, Gerlt JA, Rayment I (1998). "Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida." Biochemistry 37(41);14358-68. PMID: 9772161
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