This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two al ...
This entry represents the ACT domain, which is found twice in Aspartate kinase from Methanocaldococcus jannaschii, the enzyme that catalyses the phosphorylation of aspartic acid [6]. This domain folds as a four-stranded antiparallel sheet with two alpha-helices parallel to the sheet and located on one side of the sheet [1].
This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulati ...
This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585