Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus

Kenji Inagaki; Takeshi Nakamura; Ritsuko Maeda; Takashi Tamura; Hidehiko Tanaka

doi:10.1016/S1389-1723(00)80094-8

Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus

Kenji Inagaki, Takeshi Nakamura, Ritsuko Maeda, Takashi Tamura, Hidehiko Tanaka

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

17 Citations (Scopus)

Abstract

We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75°C, and remained active after incubation at 80°C for 30 min.

Original language	English
Pages (from-to)	344-346
Number of pages	3
Journal	Journal of Bioscience and Bioengineering
Volume	90
Issue number	3
DOIs	https://doi.org/10.1016/S1389-1723(00)80094-8
Publication status	Published - Sept 2000

Keywords

Alanine racemase
Extreme thermophile
Thermus thermophilus

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1016/S1389-1723(00)80094-8

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abstract = "We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75°C, and remained active after incubation at 80°C for 30 min.",

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AU - Inagaki, Kenji

AU - Nakamura, Takeshi

AU - Maeda, Ritsuko

AU - Tamura, Takashi

AU - Tanaka, Hidehiko

PY - 2000/9

Y1 - 2000/9

N2 - We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75°C, and remained active after incubation at 80°C for 30 min.

AB - We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75°C, and remained active after incubation at 80°C for 30 min.

KW - Alanine racemase

KW - Extreme thermophile

KW - Thermus thermophilus

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ER -

Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus

Abstract

Keywords

ASJC Scopus subject areas

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