| Type: | Family | Name: | Phosphoserine aminotransferase |
| Description: | Phosphoserine aminotransferase (PSAT) is involved in serine biosynthesis [, ]. The enzyme catalyses the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine. PSAT from Escherichia colihas been shown to be a homodimer of Mr79,000 with a conserved lysine that binds covalently to pyridoxal phosphate (PLP). PSAT is a vitamin B6-dependent enzyme and belongs to the alpha family of PLP enzymes. PSAT is also classified as a member of the aspartate aminotransferase family of PLP enzymes []. According to the structural classification of PLP-dependent enzymes [], PSAT belongs to the fold type I, where it is allocated to a separated subclass. The mechanism of action in all these enzymes is similar: PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which, depending on the reaction, is the substrate in four kinds of reactions: transamination (movement of amino groups), racemization (redistribution of enantiomers), decarboxylation (removing COOH groups), and various side-chain reactions depending on the enzyme involved. | Short Name: | Pser_aminoTfrase |
