Isolation and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing) from Alcaligenes faecalis N-38A

Biosci Biotechnol Biochem. 1995 Oct;59(10):2010-2. doi: 10.1271/bbb.59.2010.

Abstract

A screening test was undertaken to isolate a microorganism that produced 5-oxoprolinase (without ATP-hydrolyzing). The 5-oxoprolinase (without ATP-hydrolyzing) activity (decyclization activity toward L-pyroglutamate) was found in a cell-free extract of Alcaligenes faecalis N-38A, newly isolated from a soil sample. The enzyme was purified as a homogeneous preparation. The molecular weight of the enzyme was estimated to be 47,000. The decyclization activity was specific for L-pyroglutamate, and independent of ATP and metal ions. The reaction was a reversible one, i.e., cyclization reaction of L-glutamate to yield pyroglutamate was identified.

MeSH terms

  • Alcaligenes / enzymology*
  • Glutamic Acid / metabolism
  • Pyrrolidonecarboxylic Acid / isolation & purification
  • Pyrrolidonecarboxylic Acid / metabolism*
  • Substrate Specificity

Substances

  • Glutamic Acid
  • Pyrrolidonecarboxylic Acid