Characterization of ligV Essential for Catabolism of Vanillin by Sphingomonas paucimobilis SYK-6

• MASAI Eiji

  Department of Bioengineering, Nagaoka University of Technology

• YAMAMOTO Yuko

  Department of Bioengineering, Nagaoka University of Technology

• INOUE Tomohiko

  Department of Bioengineering, Nagaoka University of Technology

• TAKAMURA Kazuhiro

  Department of Bioengineering, Nagaoka University of Technology

• HARA Hirofumi

  Department of Bioengineering, Nagaoka University of Technology

• KASAI Daisuke

  Department of Bioengineering, Nagaoka University of Technology

• KATAYAMA Yoshihiro

  Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology

• FUKUDA Masao

  Department of Bioengineering, Nagaoka University of Technology

Bibliographic Information

Other Title

• Characterization of<i>ligV</i>Essential for Catabolism of Vanillin by<i>Sphingomonas paucimobilis</i>SYK-6

Abstract

The vanillin dehydrogenase gene (ligV), which conferred the ability to transform vanillin into vanillate on Escherichia coli, was isolated from Sphingomonas paucimobilis SYK-6. The ligV gene consists of a 1,440-bp open reading frame encoding a polypeptide with a molecular mass of 50,301 Da. The deduced amino acid sequence of ligV showed about 50% identity with the known vanillin dehydrogenases of Pseudomonas vanillin degraders. The gene product of ligV (LigV) produced in E. coli preferred NAD⁺ to NADP⁺ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde, but the activity toward syringaldehyde was less than 5% of that toward vanillin. Insertional inactivation of ligV in SYK-6 indicated that ligV is essential for normal growth on vanillin. On the other hand, growth on syringaldehyde was only slightly affected by ligV disruption, indicating the presence of a syringaldehyde dehydrogenase gene or genes in SYK-6.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 71 (10), 2487-2492, 2007

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• <I>Sphingomonas</I>
• lignin degradation
• aldehyde dehydrogenase
• vanillin
• syringaldehyde

Details

• CRID: 1390282681456369664
• NII Article ID: 10027519937
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.70267
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 8980707
• Web Site: http://id.ndl.go.jp/bib/8980707
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I8980707
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.70267
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed