Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver

Protein Sci. 2005 Mar;14(3):791-8. doi: 10.1110/ps.041179105. Epub 2005 Feb 2.


L-serine dehydratase (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or 2-oxobutyrate. The crystal structure of L-serine dehydratase from human liver (hSDH) has been solved at 2.5 A-resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for beta-family PLP-dependent enzymes. Each monomer serves as an active unit and is subdivided into two distinct domains: a small domain and a PLP-binding domain that covalently anchors the cofactor. Both domains show the typical open alpha/beta architecture of PLP enzymes. Comparison with the rSDH-(PLP-OMS) holo-enzyme reveals a large structural difference in active sites caused by the artifical O-methylserine. Furthermore, the activity of hSDH-PLP was assayed and it proved to show catalytic activity. That suggests that the structure of hSDH-PLP is the first structure of the active natural holo-SDH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Catalytic Domain
  • Dimerization
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Humans
  • Hydrogen Bonding
  • L-Serine Dehydratase / chemistry*
  • L-Serine Dehydratase / metabolism
  • Liver / enzymology*
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Pyridoxal Phosphate / metabolism*
  • Rats
  • Sequence Alignment
  • Water / metabolism


  • Water
  • Pyridoxal Phosphate
  • L-Serine Dehydratase