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

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	1489-1492
Number of pages	4
Journal	Bioscience, biotechnology, and biochemistry
Volume	59
Issue number	8
DOIs	https://doi.org/10.1271/bbb.59.1489
Publication status	Published - 1995
Externally published	Yes

All Science Journal Classification (ASJC) codes

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

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

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",

year = "1995",

doi = "10.1271/bbb.59.1489",

language = "English",

volume = "59",

pages = "1489--1492",

journal = "Bioscience, Biotechnology and Biochemistry",

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T1 - Metal-characterization of N-Acyl-D-glutamate Amidohydrolase from Pseudomonas sp. Strain 5f-1

AU - Wakayama, Mamoru

AU - Miura, Yasushi

AU - Oshima, Koji

AU - Sakai, Kenji

AU - Moriguchi, Mitsuaki

PY - 1995

Y1 - 1995

N2 - 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.

AB - 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.

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C2 - 7549100

AN - SCOPUS:0029347139

SN - 0916-8451

VL - 59

SP - 1489

EP - 1492

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 8

ER -

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

Abstract

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