This entry represents the C-terminal domain of Galactarate dehydratase (GarD). GarD catalyses the dehydration of galactarate to 5-dehydro-4-deoxy-D-galactarate. In the crystal structure, GarD forms dimers and each monomer consists of three domains: t ...
This entry represents the C-terminal domain of Galactarate dehydratase (GarD). GarD catalyses the dehydration of galactarate to 5-dehydro-4-deoxy-D-galactarate. In the crystal structure, GarD forms dimers and each monomer consists of three domains: the N-terminal SAF domain (Pfam:PF08666) connected to the second domain (Pfam:PF04295) through a long linker and the C-terminal domain which represents the core of the protein. This domain adopts a variant of a Rossmann fold with an unusual crossover, consisting of seven-stranded parallel beta-sheets surrounded by nine alpha-helices [1]. This domain may contain a catalytic metal binding site [1].
D-galactarate dehydratase/Altronate hydrolase, second domain
This entry includes D-galactarate dehydratase (GarD, EC:4.2.1.42) which catalyses the reaction D-galactarate = 5-keto-4-deoxy-D glucarate + H2O, [1] and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyses D-altronate = 2-keto-2 ...
This entry includes D-galactarate dehydratase (GarD, EC:4.2.1.42) which catalyses the reaction D-galactarate = 5-keto-4-deoxy-D glucarate + H2O, [1] and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyses D-altronate = 2-keto-2- deoxygluconate + H2O [2]. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core [3]. GarD structure revealed that it is a dimer in solution; each monomer has three domains, an N-terminal SAF domain (Pfam:PF08666), a second domain represented in this entry and a C-terminal domain [5]. This domain consists of three parallel beta-strands, surrounded by three alpha-helices and it interacts with the C-terminal domain from the second chain to form a dimerisation surface [5].
This entry represents the C-terminal domain of Galactarate dehydratase (GarD). GarD catalyses the dehydration of galactarate to 5-dehydro-4-deoxy-D-galactarate. In the crystal structure, GarD forms dimers and each monomer consists of three domains: t ...
This entry represents the C-terminal domain of Galactarate dehydratase (GarD). GarD catalyses the dehydration of galactarate to 5-dehydro-4-deoxy-D-galactarate. In the crystal structure, GarD forms dimers and each monomer consists of three domains: the N-terminal SAF domain (Pfam:PF08666) connected to the second domain (Pfam:PF04295) through a long linker and the C-terminal domain which represents the core of the protein. This domain adopts a variant of a Rossmann fold with an unusual crossover, consisting of seven-stranded parallel beta-sheets surrounded by nine alpha-helices [1]. This domain may contain a catalytic metal binding site [1].
D-galactarate dehydratase/Altronate hydrolase, second domain
This entry includes D-galactarate dehydratase (GarD, EC:4.2.1.42) which catalyses the reaction D-galactarate = 5-keto-4-deoxy-D glucarate + H2O, [1] and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyses D-altronate = 2-keto-2 ...
This entry includes D-galactarate dehydratase (GarD, EC:4.2.1.42) which catalyses the reaction D-galactarate = 5-keto-4-deoxy-D glucarate + H2O, [1] and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyses D-altronate = 2-keto-2- deoxygluconate + H2O [2]. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core [3]. GarD structure revealed that it is a dimer in solution; each monomer has three domains, an N-terminal SAF domain (Pfam:PF08666), a second domain represented in this entry and a C-terminal domain [5]. This domain consists of three parallel beta-strands, surrounded by three alpha-helices and it interacts with the C-terminal domain from the second chain to form a dimerisation surface [5].
