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Alanine Racemase from an Acidophile, Acidiphilium organovorum: Purification and Characterization.

T K Seow¹, K Inagaki¹, T Tamura¹

¹a Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University.

Bioscience, Biotechnology, and Biochemistry

|July 9, 2016

Summary

This study purified alanine racemase from Acidiphilium organovorum 13H. The enzyme, requiring pyridoxal 5'-phosphate (PLP), showed optimal activity at pH 9 and high temperatures, indicating cytoplasmic localization.

Keywords:

Acidiphilium organovorum acidophile alanine racemase pyridoxal 5′-phosphate

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Area of Science:

Biochemistry
Enzymology
Microbiology

Background:

Alanine racemase (EC 5.1.1.1) is crucial for bacterial cell wall synthesis.
Understanding enzyme properties from extremophiles offers insights into protein adaptation.

Purpose of the Study:

To purify and characterize alanine racemase from the acidophilic bacterium Acidiphilium organovorum 13H.
To investigate the enzyme's structural, kinetic, and cofactor requirements.

Main Methods:

Enzyme purification techniques.
Enzyme activity assays across various pH and temperature conditions.
Spectrophotometric analysis and cofactor dependency studies.

Main Results:

Purified alanine racemase exhibited a dimeric structure (33,000 M r per subunit).
Optimal activity observed at pH 9 and 50-60°C, with significant heat stability.
The enzyme requires pyridoxal 5 omino-phosphate (PLP) as a cofactor, with 2 moles of PLP per mole of enzyme.

Conclusions:

Alanine racemase from A. organovorum 13H, despite the organism's acidophilic nature, functions optimally under neutral to alkaline conditions, suggesting cytoplasmic localization.
The enzyme's thermostability and PLP dependency are key characteristics.
This enzyme exclusively catalyzes the reversible racemization of alanine.