Ontology highlight
ABSTRACT:
SUBMITTER: Koper K
PROVIDER: S-EPMC9309667 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
Koper Kaan K Han Sang-Woo SW Pastor Delia Casas DC Yoshikuni Yasuo Y Maeda Hiroshi A HA
The Journal of biological chemistry 20220611 8
Aminotransferases (ATs) are pyridoxal 5'-phosphate-dependent enzymes that catalyze the transamination reactions between amino acid donor and keto acid acceptor substrates. Modern AT enzymes constitute ∼2% of all classified enzymatic activities, play central roles in nitrogen metabolism, and generate multitude of primary and secondary metabolites. ATs likely diverged into four distinct AT classes before the appearance of the last universal common ancestor and further expanded to a large and diver ...[more]