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Volume 150, Issue 12

Characterization of -glutamyltransferase and its involvement in the degradation of capsule poly--glutamate Free

Abstract

During early stationary phase, NAFM5 produces capsular poly(-glutamic acid) (PGA, 2×10 Da), which contains - and -glutamate, and then degrades it during late stationary phase. The -glutamyltransferase (EC 2.3.2.2; GGT) of this strain successively hydrolysed PGA from the amino-terminal end, to yield both - and -glutamate. This enzyme was specifically synthesized during the stationary phase through transcriptional activation of the corresponding gene by the ComQXPA quorum-sensing system. A knockout mutant degraded PGA into 1×10 Da fragments, but not any further, indicating that the capsule PGA is first internally degraded by an endo-type of PGA hydrolase into 1×10 Da intermediates, then externally into glutamates via GGT. Due to its inability to generate the glutamates from the capsule, the mutant sporulated more frequently than the wild-type strain. The results show that GGT has a powerful exo--glutamyl hydrolase activity that participates in capsule PGA degradation to supply stationary-phase cells with constituent glutamates.

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Keyword(s): GGT, γ-glutamyltransferase , γGNA, γ-glutamyl-p-nitroanilide and γPGA, poly(γ-glutamic acid)
© SGM
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2004-12-01
2024-04-20
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Characterization of Bacillus subtilisγ-glutamyltransferase and its involvement in the degradation of capsule poly-γ-glutamate
Microbiology 150, 4115 (2004); https://doi.org/10.1099/mic.0.27467-0
/content/journal/micro/10.1099/mic.0.27467-0
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