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4-Pyridoxolactonase from a symbiotic nitrogen-fixing bacterium Mesorhizobium loti: Cloning, expression, and characterization by Junichi Funami; Yu Yoshikane; Hitoshi Kobayashi; Nana Yokochi; Baiqiang Yuan; Kozo Iwasaki; Kouhei Ohnishi; Toshiharu Yagi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is 4-Pyridoxolactonase from a symbiotic nitrogen-fixing bacterium Mesorhizobium loti: Cloning, expression, and characterization about?

4-Pyridoxolactonase is involved in the degradation pathway for pyridoxine, a free form of vitamin B 6 . The gene (mlr6805) encoding the putative 4-pyridoxolactonase of nitrogen fixing symbiotic microorganism Mesorhizobium loti MAFF303099 has been identified based on the genome database. The gene was cloned and overexpressed in a cotransformant Escherichia coli cell. The recombinant enzyme was dimeric protein and contained one mole of Zn 2+ per mole of subunit. The enzyme showed about 30% identity with various N-acylhomoserine lactone lactonases and metallo-h-lactamases. The phylogram made with ClustalW shows that 4-pyridoxolactonase makes a cluster with Agrobacterium tumefaciens acyl-homoserine lactone lactonase. The alignment of amino acid sequences suggests that 4-pyridoxolactonase has three histidine residues probably involved in binding of Zn 2+ .

Who reads 4-Pyridoxolactonase from a symbiotic nitrogen-fixing bacterium Mesorhizobium loti: Cloning, expression, and characterization?

Author

Junichi Funami; Yu Yoshikane; Hitoshi Kobayashi; Nana Yokochi; Baiqiang Yuan; Kozo Iwasaki; Kouhei Ohnishi; Toshiharu Yagi

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1570-9639)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)