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

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

doi:10.1271/bbb.59.1489

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

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

研究成果: Contribution to journal › Article › 査読

13 被引用数 (Scopus)

抄録

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.

本文言語	英語
ページ（範囲）	1489-1492
ページ数	4
ジャーナル	Bioscience, biotechnology, and biochemistry
巻	59
号	8
DOI	https://doi.org/10.1271/bbb.59.1489
出版ステータス	出版済み - 1995
外部発表	はい

All Science Journal Classification (ASJC) codes

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

文献へのアクセス

10.1271/bbb.59.1489

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引用スタイル

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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.",

author = "Mamoru Wakayama and Yasushi Miura and Koji Oshima and Kenji Sakai and Mitsuaki Moriguchi",

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AU - Oshima, Koji

AU - Sakai, Kenji

AU - Moriguchi, Mitsuaki

PY - 1995

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