PlumX Metrics
Embed PlumX Metrics

Gene cloning, purification, and characterization of α-methylserine aldolase from Bosea sp. AJ110407 and its applicability for the enzymatic synthesis of α-methyl- l -serine and α-ethyl- l -serine

Journal of Molecular Catalysis B: Enzymatic, ISSN: 1381-1177, Vol: 59, Issue: 4, Page: 237-242
2009
  • 19
    Citations
  • 0
    Usage
  • 7
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    19
    • Citation Indexes
      19
  • Captures
    7

Article Description

The gene encoding α-methylserine aldolase was isolated from Bosea sp. AJ110407. Sequence analysis revealed that the predicted amino acid sequence encoded by the 1320-bp open reading frame was 65.0% similar to the corresponding sequence of the enzyme isolated from Ralstonia sp. AJ110405. The gene was expressed in Escherichia coli, and the recombinant enzyme was purified. Gel filtration revealed the molecular mass of the purified enzyme to be approximately 78 kDa, suggesting that the enzyme is a homodimer. The enzyme exhibited a specific peak at 429 nm in the spectrum and contained 1 mol pyridoxal 5′-phosphate per mole of the subunit. The V max value was 1.40 μmol min −1 mg −1, and the K m value was 1.5 mM for the reaction wherein formaldehyde was released from α-methyl- l -serine. This enzyme could also catalyze the reverse reaction, i.e., the synthesis of α-methyl- l -serine from l -alanine and formaldehyde. This activity was inhibited in the excess of formaldehyde; however, α-methyl- l -serine was efficiently produced from l -alanine in the presence of formaldehyde. This method was also applicable for producing α-ethyl- l -serine from l -2-aminobutyric acid.

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know