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Bioscience, Biotechnology, and Biochemistry Volume 80, 2016 - Issue 5
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Biochemistry & Molecular Biology

Identification of the Fluvirucin B2 (Sch 38518) Biosynthetic Gene Cluster from Actinomadura fulva subsp. indica ATCC 53714: substrate Specificity of the β-Amino Acid Selective Adenylating Enzyme FlvNFootnote

Akimasa MiyanagaDepartment of Chemistry, Tokyo Institute of Technology, Tokyo, Japan
,
Yuki HayakawaDepartment of Chemistry and Materials Science, Tokyo Institute of Technology, Tokyo, Japan
,
Mario NumakuraDepartment of Chemistry, Tokyo Institute of Technology, Tokyo, Japan
,
Junko HashimotoJapan Biological Informatics Consortium, Tokyo, Japan
,
Kuniko TeruyaOkinawa Biotechnology Business Support Center, Okinawa Institute of Advanced Sciences, Uruma, Japan
,
Takashi HiranoOkinawa Biotechnology Business Support Center, Okinawa Institute of Advanced Sciences, Uruma, Japan;Okinawa Biotechnology Business Support Center, Okinawa Science and Technology Promotion Center, Uruma, Japan
,
Kazuo Shin-yaNational Institute of Advanced Industrial Science and Technology, Tokyo, Japan
,
Fumitaka KudoDepartment of Chemistry, Tokyo Institute of Technology, Tokyo, Japan
&
Tadashi EguchiDepartment of Chemistry and Materials Science, Tokyo Institute of Technology, Tokyo, JapanCorrespondence[email protected]
 show all
Pages 935-941 | Received 17 Nov 2015, Accepted 02 Dec 2015, Published online: 28 Jan 2016

Figures & data

Fig. 1. Fluvirucins and related β-amino acid-containing macrolactams.

Fig. 1. Fluvirucins and related β-amino acid-containing macrolactams.

Table 1. Fluvirucin B2 biosynthetic genes from Actinomadula fulva ATCC 53714 and putative functions.

Fig. 2. Amino acid selectivity of FlvN. FlvN was reacted with 0.5 mM amino acid. The bar diagram represents the relative adenylation activities. The specific activity for l-aspartate (5.4 min−1) is defined as 100% relative activity. Error bars represent SEM (n = 3).

Fig. 2. Amino acid selectivity of FlvN. FlvN was reacted with 0.5 mM amino acid. The bar diagram represents the relative adenylation activities. The specific activity for l-aspartate (5.4 min−1) is defined as 100% relative activity. Error bars represent SEM (n = 3).

Fig. 3. Proposed biosynthetic pathway of fluvirucin B2.

Fig. 3. Proposed biosynthetic pathway of fluvirucin B2.
Supplemental material

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Related Research Data

Identification of the Fluvirucin B2 (Sch 38518) Biosynthetic Gene Cluster from Actinomadura fulva subsp. indica ATCC 53714: substrate Specificity of the β-Amino Acid Selective Adenylating Enzyme FlvN
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