The role of firefly luciferase C-terminal domain in efficient coupling of adenylation and oxidative steps

被引：21

作者：

Ayabe, K

Zako, T

Ueda, H

机构：

[1] Univ Tokyo, Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, Tokyo 1138656, Japan

[2] PRESTO, Japan Sci & Technol Agcy, Kawaguchi, Saitama 3320012, Japan

来源：

FEBS LETTERS | 2005年 / 579卷 / 20期

关键词：

bioluminescence; luciferase; acyl-adenylate; reaction intermediate;

D O I：

10.1016/j.febslet.2005.07.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The N-terminal domain (N-domain) of the firefly luciferase from Photinus pyraris has weak luminescence activity, and shows a unique light emitting profile with very long rise time of more than several minutes. Through a sensitive assay of the reaction intermediate luciferyl-adenylate (LH2-AMP), we found that the slow increase in the N-domain luminescence faithfully reflected the concentration of dissociated LH2-AMP. No such correlation was observed for wild-type or mutant enzymes with short rise time, except one with longer rise time. The results suggest that the C-terminal domain plays an indispensable role in efficiently coupling adenylation and oxidative steps. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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页码：4389 / 4394

页数：6

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