F
IPR022278

Phosphoserine aminotransferase

InterPro entry
Short namePser_aminoTfrase
Overlapping
homologous
superfamilies
 
family relationships

Description

Phosphoserine aminotransferase (PSAT) is involved in serine biosynthesis
[2, 3]
. The enzyme catalyses the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine. PSAT from Escherichia coli has 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
[1]
. According to the structural classification of PLP-dependent enzymes
[4]
, PSAT belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold 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.

References

1.Structure, evolution and action of vitamin B6-dependent enzymes. Jansonius JN. Curr. Opin. Struct. Biol. 8, 759-69, (1998). View articlePMID: 9914259

2.Dysregulation of serine biosynthesis contributes to the growth defect of a Mycobacterium tuberculosis crp mutant. Bai G, Schaak DD, Smith EA, McDonough KA. Mol. Microbiol. 82, 180-98, (2011). View articlePMID: 21902733

3.Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways. Ali V, Nozaki T. Mol. Biochem. Parasitol. 145, 71-83, (2006). View articlePMID: 16289358

4.Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Grishin NV, Phillips MA, Goldsmith EJ. Protein Sci. 4, 1291-304, (1995). View articlePMID: 7670372

GO terms

Cross References

Contributing Member Database Entries
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