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Related Experiment Videos

Acid phosphatase/phosphotransferases from enteric bacteria.

Y Mihara1, T Utagawa, H Yamada

  • 1Applied Microbiology Laboratory, Ajinomoto Co., Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi 210-8681, Japan. yasuhiro_mahara@ajinomoto.com

Journal of Bioscience and Bioengineering
|October 20, 2005
PubMed
Summary
This summary is machine-generated.

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Researchers explored acid phosphatases from various bacteria, finding that enzymes from Providencia stuartii and Morganella morganii efficiently produce inosine-5'-monophosphate (5'-IMP) via pyrophosphate-nucleoside phosphotransferase activity.

Area of Science:

  • Enzymology
  • Microbial biochemistry
  • Molecular biology

Background:

  • Morganella morganii phoC acid phosphatase displays pyrophosphate (PP(i))-nucleoside phosphotransferase activity.
  • Acid phosphatases are crucial enzymes in various biological processes.

Purpose of the Study:

  • To isolate and characterize acid phosphatases with regioselective phosphotransferase activity (AP/PTase) from bacterial species.
  • To compare the enzymatic characteristics and primary structures of these enzymes with M. morganii AP/PTase.
  • To investigate the synthesis of inosine-5 '-monophosphate (5 '-IMP) using these enzymes.

Main Methods:

  • Gene isolation of AP/PTase from Providencia stuartii, Enterobacter aerogenes, Escherichia blattae, and Klebsiella planticola.
  • Comparative analysis of primary structures and enzymatic properties.

Related Experiment Videos

  • Assessment of 5 '-IMP production in E. coli overexpressing the isolated acid phosphatases.

    • Main Results:

    • Isolated AP/PTases showed high homology with M. morganii AP/PTase and belong to class A1 acid phosphatases.
    • The P. stuartii enzyme demonstrated high 5 '-IMP productivity, comparable to the M. morganii enzyme.
    • Enzymes from E. aerogenes, E. blattae, and K. planticola exhibited lower 5 '-IMP productivity, suggesting K(m) values influence efficiency.

    Conclusions:

    • Bacterial AP/PTases share significant structural homology but exhibit varying efficiencies in nucleotide synthesis.
    • Differences in nucleotide production efficiency are likely due to local sequence variations within the enzyme's binding pocket.
    • Optimizing K(m) values is critical for enhancing nucleotide production using these phosphotransferase enzymes.