Dataset Information

Biodegradation of α-endosulfan via hydrolysis pathway by Stenotrophomonas maltophilia OG2.

ABSTRACT: Stenotrophomonas maltophilia OG2 was isolated from the intestine of cockroaches that was collected from a cow barn contaminated some pesticides belong to pyrethroid and organochlorine groups. OG2 was able to degrade α-endosulfan in non sulfur medium (NSM) as a sole sulfur source for growth within 10 days of incubation. The effects of some growth parameters on endosulfan biodegradation by OG2 was studied and found that the biodegradation was significantly affected by the endosulfan concentrations, pH and temperature. Experimental results obtained in different conditions show that the optimum concentration of α-endosulfan, pH and temperature were 100 mg/L, 8.0 and 30 °C, respectively. Under these conditions, the bacterium degraded 81.53% of the α-endosulfan after 10 days. The concentration of α-endosulfan and its metabolites was determined by HPLC. Endosulfan ether, endosulfan lactone and endosulfan diol were the main metabolites in culture, but did not produce toxic metabolite, endosulfan sulfate. These results suggested that S. maltophilia OG2 degrades α-endosulfan via a hydrolysis pathway. The present study indicates that strain OG2 may have potential use in the biodegradation of pesticides contaminated environments.

SUBMITTER: Ozdal M

PROVIDER: S-EPMC5451363 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Biodegradation of α-endosulfan via hydrolysis pathway by Stenotrophomonas maltophilia OG2.

Ozdal Murat M Ozdal Ozlem Gur OG Algur Omer Faruk OF Kurbanoglu Esabi Basaran EB

3 Biotech 20170531 2

Stenotrophomonas maltophilia OG2 was isolated from the intestine of cockroaches that was collected from a cow barn contaminated some pesticides belong to pyrethroid and organochlorine groups. OG2 was able to degrade α-endosulfan in non sulfur medium (NSM) as a sole sulfur source for growth within 10 days of incubation. The effects of some growth parameters on endosulfan biodegradation by OG2 was studied and found that the biodegradation was significantly affected by the endosulfan concentrations ...[more]

PMID: 28567625

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Project description:PabB, aminodeoxychorismate synthase, is the chorismic acid binding component of the heterodimeric PabA-PabB complex that converts chorismic acid to 4-amino-4-deoxychorismate, a precursor of p-aminobenzoate and folic acid in microorganisms. The second component, a glutamine amidotransferase subunit, PabA, generates ammonia that is channeled to the PabB active site where it attacks C4 of a chorismate-derived intermediate that is covalently bound, through C2, to an active site lysine residue. The presence of a PIKGT motif was, until recently, believed to allow discrimination of PabB enzymes from the closely related enzyme anthranilate synthase, which typically contains a PIAGT active site motif and does not form a covalent enzyme-substrate intermediate with chorismate. A subclass of PabB enzymes that employ an alternative mechanism requiring 2 equiv of ammonia from glutamine and that feature a noncovalently bound 2-amino-2-deoxyisochorismate intermediate was recently identified. Here we report the 2.25 Å crystal structure of PabB from the emerging pathogen Stenotrophomonas maltophilia. It is the first reported structure of a PabB that features the PIAGT motif. Surprisingly, no dedicated pabA is evident in the genome of S. maltophilia, suggesting that another cellular amidotransferase is able to fulfill the role of PabA in this organism. Evaluation of the ammonia-dependent aminodeoxychorismate synthase activity of S. maltophilia PabB alone revealed that it is virtually inactive. However, in the presence of a heterologous PabA surrogate, typical levels of activity were observed using either glutamine or ammonia as the nitrogen source. Additionally, the structure suggests that a key segment of the polypeptide can remodel itself to interact with a nonspecialized or shared amidotransferase partner in vivo. The structure and mass spectral analysis further suggest that S. maltophilia PabB, like Escherichia coli PabB, binds tryptophan in a vestigial regulatory site. The observation that the binding site is unoccupied in the crystal structure, however, suggests the affinity may be low relative to that of E. coli PabB.

Dataset Information

Biodegradation of α-endosulfan via hydrolysis pathway by Stenotrophomonas maltophilia OG2.

Publications

Biodegradation of α-endosulfan via hydrolysis pathway by Stenotrophomonas maltophilia OG2.

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