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Microbiology Society logo Microbiology

Volume 149, Issue 3

Identification of the putrescine biosynthetic genes in and characterization of agmatine deiminase and -carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway Free

Abstract

Putrescine can be synthesized either directly from ornithine by ornithine decarboxylase (ODC; the product) or indirectly from arginine via arginine decarboxylase (ADC; the product). The authors identified the and genes in PAO1. The activities of the two decarboxylases were similar and each enzyme alone appeared to direct sufficient formation of the polyamine for normal growth. A mutant defective in both and was a putrescine auxotroph. In this strain, agmatine deiminase (the product) and -carbamoylputrescine amidohydrolase (the product), which were initially identified as the catabolic enzymes of agmatine, biosynthetically convert agmatine to putrescine in the ADC pathway: a double mutant of and was a putrescine auxotroph. AguA was purified as a homodimer of 43 kDa subunits and AguB as a homohexamer of 33 kDa subunits. AguA specifically deiminated agmatine with and values of 0·6 mM and 4·2 s, respectively. AguB was specific to -carbamoylputrescine and the and values of the enzyme for the substrate were 0·5 mM and 3·3 s, respectively. Whereas AguA has no structural relationship to any known C–N hydrolases, AguB is a protein of the nitrilase family that performs thiol-assisted catalysis. Inhibition by SH reagents and the conserved cysteine residue in AguA and its homologues suggested that this enzyme is also involved in thiol-mediated catalysis.

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Keyword(s): ADC, arginine decarboxylase and ODC, ornithine decarboxylase
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2003-03-01
2025-01-25
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/content/journal/micro/10.1099/mic.0.26009-0
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Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway
Microbiology 149, 707 (2003); https://doi.org/10.1099/mic.0.26009-0
/content/journal/micro/10.1099/mic.0.26009-0
/content/journal/micro/10.1099/mic.0.26009-0
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