Details

Autor(en) / Beteiligte

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

Titel

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

Ist Teil von

• Biochimica et biophysica acta, 2005-12, Vol.1753 (2), p.234-239

Ort / Verlag

Netherlands: Elsevier B.V

Erscheinungsjahr

2005

Quelle

MEDLINE

Beschreibungen/Notizen

• 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-β-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+.