Literature DB >> 8535001

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

S Murao1, A Nishimura, Y Ozaki, H Oyama, T Shin.   

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.

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Year:  1995        PMID: 8535001     DOI: 10.1271/bbb.59.2010

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  2 in total

1.  Molecular cloning, sequencing, and expression in Escherichia coli of the gene encoding a novel 5-oxoprolinase without ATP-hydrolyzing activity from Alcaligenes faecalis N-38A.

Authors:  A Nishimura; H Oyama; T Hamada; K Nobuoka; T Shin; S Murao; K Oda
Journal:  Appl Environ Microbiol       Date:  2000-08       Impact factor: 4.792

2.  Purification and characterization of a novel 5-oxoprolinase (without ATP-hydrolyzing activity) from Alcaligenes faecalis N-38A.

Authors:  A Nishimura; Y Ozaki; H Oyama; T Shin; S Murao
Journal:  Appl Environ Microbiol       Date:  1999-02       Impact factor: 4.792

  2 in total

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