Gene cloning and characterization of a vanadium-dependent bromoperoxidase from the red alga Laurencia saitoi, a producer of brominated diterpenoids and triterpenoids

Kaneko, Kensuke; Kobayashi, Daiki; Masaki, Shiro; Washio, Kenji; Morikawa, Masaaki; Okino, Tatsufumi

Gene cloning and characterization of a vanadium-dependent bromoperoxidase from the red alga Laurencia saitoi, a producer of brominated diterpenoids and triterpenoids

Kaneko, Kensuke; Kobayashi, Daiki; Masaki, Shiro et al.

Journal of Applied Phycology, 2023, 35, 1443-1452

Permalink : https://hdl.handle.net/2115/91590

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アクセス権	open access
URI	https://hdl.handle.net/2115/91590
タイトル	Gene cloning and characterization of a vanadium-dependent bromoperoxidase from the red alga Laurencia saitoi, a producer of brominated diterpenoids and triterpenoids
著者	Kaneko, Kensuke ; Kobayashi, Daiki ; Masaki, Shiro ; Washio, Kenji ; Morikawa, Masaaki ; Okino, Tatsufumi
著者名 Kaneko, Kensuke
著者名 Kobayashi, Daiki
著者名 Masaki, Shiro
e-Rad_Researcher 50241302 著者名 Washio, Kenji
e-Rad_Researcher 20230104 著者名 Morikawa, Masaaki
e-Rad_Researcher 30280910 著者名 Okino, Tatsufumi
言語	英語
キーワード	Laurencia saitoi
	Vanadium-dependent bromoperoxidase (V-BPO)
	Bromination activity
	Rhodophyta
発行日	2023-04-10
出版者	Springer
収録物名	Journal of Applied Phycology
巻(号)	35
ページ	1443-1452
抄録	The gene encoding vanadium-dependent bromoperoxidase (V-BPO) was cloned for the first time from the red alga Laurencia saitoi, which produces pharmaceutically promising brominated diterpenoids and triterpenoids. The molecular weight of V-BPO from L. saitoi (LsVBPO1) was the highest (77.0 kDa) among previously reported V-BPOs from Laurencia with a peptide insertion Asn194-Ser221 containing short Gln repeats. It shares approximately 60% amino acid sequence identity with V-BPOs from L. nipponica (LnVBPO1 and LnVBPO2) and L. okamurae (LoVBPO1a and LoVBPO2a). Heterologously expressed LsVBPO1 in Escherichia coli was partially purified and exhibited low but significant bromination activity of 38 U mg(-1) protein using monochlorodimedone. The pH optimum was 8.0, which was more alkaline than that for LnVBPOs and LoVBPO2a (pH 7.0). The K-m for H2O2 was 0.04 mM, comparable to LnVBPO1 (0.026 mM), LnVBPO2 (0.025 mM), and LoVBPO2a (0.014 mM). LsVPBO1 retained its bromination activity until 45 degrees C for 20 min. When incubated at 55 degrees C for 20 min, catalytic activity decreased rapidly, as shown for LnVBPO1 and LoVBPO2a (retained at 45 degrees C, decreased at 55 degrees C) and LnVBPO2 (retained at 55 degrees C, decreased at 65 degrees C). Unlike other V-BPOs from Laurencia (LnVBPO1, LnVBPO2, and LoVBPO2a), dialysis and concentration during purification process were rapidly inactivated LsVBPO1, suggesting its structural instability.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	This version of the article has been accepted for publication, after peer review (when applicable) and is subject to Springer Nature’s AM terms of use, but is not the Version of Record and does not reflect post-acceptance improvements, or any corrections. The Version of Record is available online at: http://dx.doi.org/10.1007/s10811-023-02953-w
PISSN	0921-8971
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1007/s10811-023-02953-w