Abstract
We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed an optimum reaction pH at around 9.0 and were stimulated 5- to 7-fold by such divalent cations as Mg++, Mn++ and Ca++.
Keywords: Human serine racemase, porin, groE, His-tag, halophile
Protein & Peptide Letters
Title: Purification and Characterization of Human Brain Serine Racemase Expressed in Moderately Halophilic Bacteria
Volume: 16 Issue: 2
Author(s): Chizuru Nagayoshi, Matsujiro Ishibashi and Masao Tokunaga
Affiliation:
Keywords: Human serine racemase, porin, groE, His-tag, halophile
Abstract: We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed an optimum reaction pH at around 9.0 and were stimulated 5- to 7-fold by such divalent cations as Mg++, Mn++ and Ca++.
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Cite this article as:
Nagayoshi Chizuru, Ishibashi Matsujiro and Tokunaga Masao, Purification and Characterization of Human Brain Serine Racemase Expressed in Moderately Halophilic Bacteria, Protein & Peptide Letters 2009; 16 (2) . https://dx.doi.org/10.2174/092986609787316261
DOI https://dx.doi.org/10.2174/092986609787316261 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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