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 journalArticle

13 Citations (Scopus)

Abstract

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
Volume59
Issue number8
DOIs
Publication statusPublished - Jan 1 1995

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Pseudomonas
Metals
Zinc
Alcaligenes
Enzyme Stability
Enzymes
Amino Acid Sequence
Catalyst activity
Amino Acids
Atoms
N-acyl-D-glutamate deacylase

All Science Journal Classification (ASJC) codes

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

Cite this

Metal-characterization of N-Acyl-D-glutamate Amidohydrolase from Pseudomonas sp. Strain 5f-1. / Wakayama, Mamoru; Miura, Yasushi; Oshima, Koji; Sakai, Kenji; Moriguchi, Mitsuaki.

In: Bioscience, biotechnology, and biochemistry, Vol. 59, No. 8, 01.01.1995, p. 1489-1492.

Research output: Contribution to journalArticle

Wakayama, Mamoru ; Miura, Yasushi ; Oshima, Koji ; Sakai, Kenji ; Moriguchi, Mitsuaki. / Metal-characterization of N-Acyl-D-glutamate Amidohydrolase from Pseudomonas sp. Strain 5f-1. In: Bioscience, biotechnology, and biochemistry. 1995 ; Vol. 59, No. 8. pp. 1489-1492.
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