2013
DOI: 10.1074/jbc.m113.477380
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Listeria monocytogenes aguA1, but Not aguA2, Encodes a Functional Agmatine Deiminase

Abstract: Background: Listeria monocytogenes has two putative agmatine deiminase homologs, AguA1 and AguA2. Results: Only AguA1, but not AguA2, acts as functional agmatine deiminase and mediates acid tolerance in L. monocytogenes. Conclusion: Provided is the first biological insight into the roles of AgDI in acid tolerance of L. monocytogenes. Significance: We have discovered a novel residue Gly-157 other than the known catalytic triad (Cys-His-Glu/Asp) critical for L. monocytogenes AgDI activity.

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Cited by 22 publications
(31 citation statements)
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“…A homologof the gene encoding agmatine deiminase, AgDI, which mediates acid tolerance in L. monocytogenes ( 33 ), was found in the E. anophelis genomes. Further studies may investigate the possible role of AgDI and potential adherence factors for vaginal colonization in E. anophelis .…”
Section: Resultsmentioning
confidence: 99%
“…A homologof the gene encoding agmatine deiminase, AgDI, which mediates acid tolerance in L. monocytogenes ( 33 ), was found in the E. anophelis genomes. Further studies may investigate the possible role of AgDI and potential adherence factors for vaginal colonization in E. anophelis .…”
Section: Resultsmentioning
confidence: 99%
“…L. monocytogenes gene deletion and complementation strategy was employed as described previously [21,22]. Upstream and downstream regions of the interest gene were overlapped using a homologous recombination strategy with an overlap extension PCR procedure (see the primers in Table 1) and cloned into the plasmid pKSV7.…”
Section: Generation Of In-frame Gene Deletion Mutant and Complementedmentioning
confidence: 99%
“…, as previously described [21]. The values K m , V max , and K cat were calculated using the software GraphPad Prism 8.0 (GraphPad Software, La Jolla, CA, USA), where [S] is the substrate concentration, v 0 the initial velocity, V max the maximum velocity, and K m the Michaelis-Menten constant.…”
Section: The Michaelis-menten Kinetic Parametersmentioning
confidence: 99%
“…Listeria monocytogenes contains several enzyme systems including F 0 F 1 -ATPase, ADI, AgDI, GAD and acid tolerance response, to maintain intracellular pH homeostasis in acidic environments [9] . Under acid stress, F 0 F 1 -ATPase system uses ATP hydrolysis to produce proton motive force to pump cytoplasmic protons, while the ADI and AgDI use arginine and agmatine to produce ammonia to neutralize the cytoplasmic protons, respectively [10,11] . The glutamate decarboxylase (GAD) system, which consumes intracellular protons by converting glutamate to γ-aminobutyrate [12] , also plays a role in acid resistance of L. monocytogenes to protect them in low pH foods.…”
Section: Introductionmentioning
confidence: 99%