Expression and characterization of Campylobacter jejuni benzoylglycine amidohydrolase (Hippuricase) gene in Escherichia coli

Hani, Eric Kurt; Chan, Vivien

doi:10.1128/jb.177.9.2396-2402.1995

Cited by 77 publications

(68 citation statements)

References 33 publications

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“…1) that includes hippuricases that cleave benzoylglycine (29) and aminoacylases that hydrolyze acetylated amino acids (27). Interestingly, an IAA-Asp hydrolase (IaaspH) purified from Enterobacter agglomerans (26,40) is ϳ20% identical to the Arabidopsis amidohydrolases characterized here (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Characterization of a Family of IAA-Amino Acid Conjugate Hydrolases from Arabidopsis

LeClere¹,

Tellez²,

Rampey³

et al. 2002

Journal of Biological Chemistry

275

283

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The mechanisms by which plants regulate levels of the phytohormone indole-3-acetic acid (IAA) are complex and not fully understood. One level of regulation appears to be the synthesis and hydrolysis of IAA conjugates, which function in both the permanent inactivation and temporary storage of auxin. Similar to free IAA, certain IAA-amino acid conjugates inhibit root elongation. We have tested the ability of 19 IAA-L-amino acid conjugates to inhibit Arabidopsis seedling root growth. We have also determined the ability of purified glutathione S-transferase (GST) fusions of four Arabidopsis IAAamino acid hydrolases (ILR1, IAR3, ILL1, and ILL2) to release free IAA by cleaving these conjugates. Each hydrolase cleaves a subset of IAA-amino acid conjugates in vitro, and GST-ILR1, GST-IAR3, and GST-ILL2 have K m values that suggest physiological relevance. In vivo inhibition of root elongation correlates with in vitro hydrolysis rates for each conjugate, suggesting that the identified hydrolases generate the bioactivity of the conjugates.

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Section: Discussionmentioning

confidence: 99%

“…Although these Arabidopsis hydrolases lack close homologs in non-plant eukaryotes, they resemble (19 -34% identical) microbial hydrolases (Fig. 1) that accept diverse substrates, including IAA-Asp (26), acetylated amino acids (27), benzyloxycarbonyl-modified amino acids (28), and benzoylglycine (29).…”

mentioning

confidence: 99%

Characterization of a Family of IAA-Amino Acid Conjugate Hydrolases from Arabidopsis

LeClere¹,

Tellez²,

Rampey³

et al. 2002

Journal of Biological Chemistry

275

283

View full text Add to dashboard Cite

show abstract

“…The strains were further confirmed as Campylobacter by biochemical tests (catalase and oxidase) and growth under microaerophilic conditions at 37 to 42°C but not at 25°C (11,13,21,25). The strains were confirmed as the C. jejuni species by hippurate hydrolysis (9,25). The cells were harvested, and the pellet was resuspended in 10 ml of brain heart infusion broth containing 10% glycerol.…”

Section: Methodsmentioning

confidence: 99%

Survival of Cold-Stressed Campylobacter jejuni on Ground Chicken and Chicken Skin during Frozen Storage

Bhaduri

Cottrell

2004

Appl Environ Microbiol

120

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Campylobacter jejuni is prevalent in poultry, but the effect of combined refrigerated and frozen storage on its survival, conditions relevant to poultry processing and storage, has not been evaluated. Therefore, the effects of refrigeration at 4°C, freezing at ؊20°C, and a combination of refrigeration and freezing on the survival of C. jejuni in ground chicken and on chicken skin were examined. Samples were enumerated using tryptic soy agar containing sheep's blood and modified cefoperazone charcoal deoxycholate agar. Refrigerated storage alone for 3 to 7 days produced a reduction in cell counts of 0.34 to 0.81 log 10 CFU/g in ground chicken and a reduction in cell counts of 0.31 to 0.63 log 10 CFU/g on chicken skin. Declines were comparable for each sample type using either plating medium. Frozen storage, alone and with prerefrigeration, produced a reduction in cell counts of 0.56 to 1.57 log 10 CFU/g in ground chicken and a reduction in cell counts of 1.38 to 3.39 log 10 CFU/g on chicken skin over a 2-week period. The recovery of C. jejuni following freezing was similar on both plating media. The survival following frozen storage was greater in ground chicken than on chicken skin with or without prerefrigeration. Cell counts after freezing were lower on chicken skin samples that had been prerefrigerated for 7 days than in those that had been prerefrigerated for 0, 1, or 3 days. This was not observed for ground chicken samples, possibly due to their composition. C. jejuni survived storage at 4 and ؊20°C with either sample type. This study indicates that, individually or in combination, refrigeration and freezing are not a substitute for safe handling and proper cooking of poultry.

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“…For differentiation of C. jejuni from C. coli, a third PCR was performed with hippuricase gene primers [29]. The hippuricase gene has been shown to be speci®c for C. jejuni [29,30] Detection of cdt genes from Campylobacter isolates by PCR and nucleotide sequencing of the cdtB gene…”

Section: Identi®cation Of Campylobacter Spp By Pcrmentioning

confidence: 99%

Prevalence of cytolethal distending toxin (cdt) genes and CDT production in Campylobacter spp. isolated from Danish broilers

Bang¹,

Scheutz

Ahrens

et al. 2001

Journal of Medical Microbiology

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Expression and characterization of Campylobacter jejuni benzoylglycine amidohydrolase (Hippuricase) gene in Escherichia coli

Cited by 77 publications

References 33 publications

Characterization of a Family of IAA-Amino Acid Conjugate Hydrolases from Arabidopsis

Characterization of a Family of IAA-Amino Acid Conjugate Hydrolases from Arabidopsis

Survival of Cold-Stressed Campylobacter jejuni on Ground Chicken and Chicken Skin during Frozen Storage

Prevalence of cytolethal distending toxin (cdt) genes and CDT production in Campylobacter spp. isolated from Danish broilers

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