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Gene Review:

PA1742 - amidotransferase

Pseudomonas aeruginosa PAO1

Bernard, D. et al., Chmara, H. et al., Chmara, H. et al.

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Disease relevance of PA1742

Asparaginyl-tRNA formation in Pseudomonas aeruginosa PAO1 involves a nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) which forms Asp-tRNA(Asp) and Asp-tRNA(Asn), and a tRNA-dependent amidotransferase which transamidates the latter into Asn-tRNA(Asn) [1].

High impact information on PA1742

It does not inhibit xanthosine 5'-monophosphate amidotransferase, glutaminase or gamma-glutamyltranspeptidase [2].
The addition of glutamine protected the amidotransferase from inactivation by anticapsin . The anticapsin was demonstrated to be a mixed type or competitive inhibitor with respect to glutamine with a Ki value of 10(-6) to 10(-7) M [3].

References

Inhibition by L-aspartol adenylate of a nondiscriminating aspartyl-tRNA synthetase reveals differences between the interactions of its active site with tRNA(Asp) and tRNA(Asn). Bernard, D., Akochy, P.M., Bernier, S., Fisette, O., Brousseau, O.C., Chênevert, R., Roy, P.H., Lapointe, J. J Enzyme Inhib Med Chem (2007) [Pubmed]
Inhibition of glucosamine-6-phosphate synthetase from bacteria by anticapsin. Chmara, H., Zähner, H., Borowski, E., Milewski, S. J. Antibiot. (1984) [Pubmed]
The inactivation of glucosamine synthetase from bacteria by anticapsin, the C-terminal epoxyamino acid of the antibiotic tetaine. Chmara, H., Zähner, H. Biochim. Biophys. Acta (1984) [Pubmed]

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