Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Piv, a site-specific invertase from Moraxella lacunata, exhibits amino acid homology with the transposases of the IS110/IS492 family of insertion elements. The functions of conserved amino acid motifs that define this novel family of both transposases and site-specific recombinases (Piv/MooV family) were examined by mutagenesis of fully conserved amino acids within each motif in Piv. All Piv mutants altered in conserved residues were defective for in vivo inversion of the M. lacunata invertible DNA segment, but competent for in vivo binding to Piv DNA recognition sequences. Although the primary amino acid sequences of the Piv/MooV recombinases do not contain a conserved DDE motif, which defines the retroviral integrase/transposase (IN/Tnps) family, the predicted secondary structural elements of Piv align well with those of the IN/Tnps for which crystal structures have been determined. Molecular modelling of Piv based on these alignments predicts that E59, conserved as either E or D in the Piv/MooV family, forms a catalytic pocket with the conserved D9 and D101 residues. Analysis of Piv E59G confirms a role for E59 in catalysis of inversion. These results suggest that Piv and the related IS110/IS492 transposases mediate DNA recombination by a common mechanism involving a catalytic DED or DDD motif.
 ...
PMID:Conserved amino acid motifs from the novel Piv/MooV family of transposases and site-specific recombinases are required for catalysis of DNA inversion by Piv. 1116 5

Piv, a unique prokaryotic site-specific DNA invertase, is related to transposases of the insertion elements from the IS110/IS492 family and shows no similarity to the site-specific recombinases of the tyrosine- or serine-recombinase families. Piv tertiary structure is predicted to include the RNase H-like fold that typically encompasses the catalytic site of the recombinases or nucleases of the retroviral integrase superfamily, including transposases and RuvC-like Holliday junction resolvases. Analogous to the DDE and DEDD catalytic motifs of transposases and RuvC, respectively, four Piv acidic residues D9, E59, D101, and D104 appear to be positioned appropriately within the RNase H fold to coordinate two divalent metal cations. This suggests mechanistic similarity between site-specific inversion mediated by Piv and transposition or endonucleolytic reactions catalyzed by enzymes of the retroviral integrase superfamily. The role of the DEDD motif in Piv catalytic activity was addressed using Piv variants that are substituted individually or multiply at these acidic residues and assaying for in vivo inversion, intermolecular recombination, and DNA binding activities. The results indicate that all four residues of the DEDD motif are required for Piv catalytic activity. The DEDD residues are not essential for inv recombination site recognition and binding, but this acidic tetrad does appear to contribute to the stability of Piv-inv interactions. On the basis of these results, a working model for Piv-mediated inversion that includes resolution of a Holliday junction is presented.
 ...
PMID:Piv site-specific invertase requires a DEDD motif analogous to the catalytic center of the RuvC Holliday junction resolvases. 1586 29

Due to the ecological toxicity and environmental residues, how to remove the persistent organic pollutants (POPs), especially of polycyclic-aromatic-hydrocarbons (PAHs) and dichloro-diphenyl-trichloroethanes (DDTs), from agricultural soil has captured the attention of scholars for a long time. To develop an effective and low-cost in situ co-remediation technique, five independent but complementary treatments were used on an over-standard PAHs-DDTs co-contaminated soil in an agricultural greenhouse. Experimental results identified that the combination of microbe (Bacillus methylotrophicus) - plant (Brassica rapa) could remove rhamnolipid activated PAHs and DDTs effectively after enhanced by Staphylococcus pasteuri. Also, the Benzoapyrene and total DDTs residue in Brassica rapa was up to the standard of National (China) food safety. The lignin enhanced the removal of high-rings PAHs and p-p' DDE but reduced soil microbial biomass carbon and soil enzymes activity (polyphenol oxidase, invertase and acid phosphatase). Pearson correlation analysis showed that polyphenol oxidase activity was significantly related to the PAHs/DDTs dissipation rate. Our research suggested a new amendment that could remediate PAHs/DDTs co-contaminated agricultural soil without interrupting crop production, and the polyphenol oxidase activity should be considered as a micro-ecological indicator in this process.
 ...
PMID:Effect of lignin and plant growth-promoting bacteria (Staphylococcus pasteuri) on microbe-plant Co-remediation: A PAHs-DDTs Co-contaminated agricultural greenhouse study. 3245 Mar 51