4.6 Article

Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in Bacillus altitudinis W3

期刊

CATALYSTS
卷 10, 期 11, 页码 -

出版社

MDPI
DOI: 10.3390/catal10111308

关键词

aminotransferase; pyridoxal 5′ -phosphate; secondary structure; conserved domain; AFM; catalytic activity; biochemical characteristics; (R)-α -phenethylamine

资金

  1. Collaborative Innovation Involving Production, Teaching & Research Funds of Jiangsu Province [BY2014023-28]
  2. Agricultural Support Project, Wuxi Science & Technology Development [CLE01N1310]

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Aminotransferases are employed as industrial biocatalysts to produce chiral amines with high enantioselectivity and yield. BpTA-1 and BpTA-2 are the only two pyridoxal 5 '-phosphate-dependent fold type IV transaminase enzymes in Bacillus altitudinis W3. Herein, we compared the structures and biochemical characteristics of BpTA-1 and BpTA-2 using bioinformatic analysis, circular dichroism spectroscopy, atomic force microscopy and other approaches. BpTA-1 and BpTA-2 are similar overall; both form homodimers and utilize a catalytic lysine. However, there are distinct differences in the substrate cofactor-binding pocket, molecular weight and the proportion of the secondary structure. Both enzymes have the same stereoselectivity but different enzymatic properties. BpTA-2 is more active under partial alkaline and ambient temperature conditions and BpTA-1 is more sensitive to pH and temperature. BpTA-2 as novel enzyme not only fills the building blocks of transaminase but also has broader industrial application potential for (R)-alpha-phenethylamines than BpTA-1. Structure-function relationships were explored to assess similarities and differences. The findings lay the foundation for modifying these enzymes via protein engineering to enhance their industrial application potential.

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