|Domain Trusted Cutoff||406.75|
|Domain Noise Cutoff||372.15|
|Entry Date||Jan 4 2007 5:03PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||In E. coli this enzyme (GarL, [1,2]) 2-dehydro-3-deoxyglucarate aldolase acts in the catabolism of several sugars including D-galactarate, D-glucarate and L-idarate. In fact, 5-dehydro-4-deoxy-D-glucarate aldolase is a synonym for this enzyme as it is unclear in the literature whether the enzyme acts on only one of these or, as seems likely, has no preference. (Despite the apparent large difference in substrate stucture indicated by their names, 2-DH-3DO- and 5-DH-4DO-glucarate differ only by the chirality of most central hydroxyl-bearing carbon and is alternately named 2-DH-3DO-galactarate.) The reported product of D-galactarate dehydratase (184.108.40.206) is the 5DH-4DO-glucarate isomer and this enzyme is found proximal to the aldolase in many genomes (GenProp0714) where no epimerase is known. Similarly, the product of D-glucarate dehydratase (220.127.116.11) is again the 5-DH-4DO isomer, so the provenance of the 2-DH-3DO-glucarate isomer for which this enzyme is named is unclear.|
RM PMID: 9772162
RT Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli.
RA Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA
RL Biochemistry. 1998 Oct 13;37(41):14369-75.
RM PMID: 10921867
RT Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.
RA Izard T, Blackwell NC
RL EMBO J. 2000 Aug 1;19(15):3849-56.
DR HAMAP; MF_01291; 22 of 24|
|Genome Property||GenProp0714: galactarate utilization via tartronate semi-aldehyde (HMM)|
| ||GenProp0716: glucarate utilization via tartronate semi-aldehyde (HMM)|
© J. Craig Venter Institute | Privacy Statement | Data Disclaimer