Metal-characterization of N-Acyl-D-glutamate Amidohydrolase from Pseudomonas sp. Strain 5f-1

Mamoru Wakayama, Yasushi Miura, Koji Oshima, Kenji Sakai, Mitsuaki Moriguchi

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


N-Acyl-D-glutamate amidohydrolase (D-AGase) from Pseudomonas sp. 5f-1 was a zinc-metalloenzyme which contained 2.06-2.61 g·atom of Zn per mole of enzyme. The zinc atom was required for the catalytic activity and stability of the enzyme. The N-terminal amino acid sequence of Pseudomonas sp. 5f-1 D-AGase showed 32% identity to that of Alcaligenes xylosoxydans subsp. xylosoxydans A-6.

Original languageEnglish
Pages (from-to)1489-1492
Number of pages4
JournalBioscience, biotechnology, and biochemistry
Issue number8
Publication statusPublished - 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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