Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme

J Biol Chem. 1982 Apr 25;257(8):4386-91.

Abstract

We have found a novel enzyme that exclusively decomposes L-selenocysteine into L-alanine and H2Se in various mammalian tissues, and have named it selenocysteine lyase. The enzyme from pig liver has been purified to homogeneity. It has a molecular weight of approximately 85,000, and contains pyridoxal 5'-phosphate as a coenzyme. Its maximum reactivity is at about pH 9.0. Balance studies showed that 1 mol of selenocysteine is converted to equimolar amounts of alanine and H2Se. The following amino acids are insert: L-cysteine, L-serine, L-cysteine sulfinate, selenocysteamine, Se-ethyl-DL-selenocysteine, and L-selenohomocysteine. L-Cysteine (Ki, 1.0 mM) competes with L-selenocysteine (Km, 0.83 mM) to inhibit the enzyme reaction. The enzyme is the first proven enzyme that specifically acts on selenium compounds.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Cysteine / analogs & derivatives
  • Cysteine / metabolism
  • Liver / enzymology*
  • Lyases / metabolism*
  • Molecular Weight
  • Selenium / metabolism
  • Selenocysteine
  • Species Specificity
  • Spectrophotometry
  • Substrate Specificity
  • Swine
  • Tissue Distribution

Substances

  • Selenocysteine
  • Lyases
  • selenocysteine lyase
  • Selenium
  • Cysteine