Cloning of 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression and sequencing of the dhlA gene

Janssen, Dick B.; Pries, Frens; Ploeg, Jan van der; Kazemier, Bert; Terpstra, Peter; Witholt, Bernard

doi:10.1128/jb.171.12.6791-6799.1989

Cited by 215 publications

(162 citation statements)

References 34 publications

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“…Moraxella B (DehH1, Genbank/EMBL Accession Number D90422; Kawasaki et al, 1992), tetrachlorocyclohexadiene dehalogenase from Sphingomonas paucimobilis (LinB, D14594; Nagata et al, 1993), and 1-chloroalkane halidohydrolase from Rhodococcus rhodochrous NCIMB13064 (DhaA, L49435; Kulakova et al, 1997) showed that they have considerable homology with DhlA (M26950), suggesting FIGURE 2: Sequence alignment of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 (DhlA; Janssen et al, 1989), haloacid dehalogenase from Moraxella B (DehH1; Kawasaki et al, 1992), tetrachlorocyclohexadiene dehalogenase from Sphingomonas paucimobilis (LinB; Nagata et al, 1993), and 1-chloroalkane halidohydrolase from Rhodococcus rhodochrous NCIMB13064 (DhaA; Kulakova et al, 1997). The sequence comparison was carried out using the program DNASTAR (DNASTAR Inc., Madison, WI).…”

Section: Sequence Alignment Of R/ -Hydrolase Fold Dehalogenases Sequmentioning

confidence: 99%

Repositioning the Catalytic Triad Aspartic Acid of Haloalkane Dehalogenase: Effects on Stability, Kinetics, and Structure

et al. 1997

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Section: Sequence Alignment Of R/ -Hydrolase Fold Dehalogenases Sequmentioning

confidence: 99%

Repositioning the Catalytic Triad Aspartic Acid of Haloalkane Dehalogenase: Effects on Stability, Kinetics, and Structure

et al. 1997

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“…2). Among these, the haloalkane dehalogenase has been studied in most detail (Janssen et al, 1989;Verschueren et al, 1993). On the basis of its three-dimensional structure it has been grouped into the superfamily of a//l-hydrolase-fold enzymes, the most prominent member of which is acetylcholine esterase (Franken et al, 1991 ;Ollis et al, 1992).…”

Section: Halomentioning

confidence: 99%

Visualization of a Covalent Intermediate between Microsomal Epoxide Hydrolase, but not Cholesterol Epoxide Hydrolase, and their Substrates

Müller

Arand

Frank

et al. 1997

European Journal of Biochemistry

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Mammalian soluble and microsomal epoxide hydrolases have been proposed to belong to the family of n/~-hydrolase-fold enzymes. These enzymes hydrolyse their substrates by a catalytic triad, with the first step of the enzymatic reaction being the formation of a covalent enzyme-substrate ester. In the present paper, we describe the direct visualization of the ester formation between rat microsomal epoxide hydrolase and its substrate. Microsomal epoxide hydrolase was precipitated with acetone after brief incubation with 11 -"C]epoxystearic acid. After denaturing SDS gel electrophoresis the protein-bound radioactivity was detected by fluorography. Pure epoxide hydrolase and crude microsomes showed a single radioactive signal of the expected molecular mass that could be suppressed by inclusion of the competitive inhibitor 1 ,I ,I -trichloropropene oxide in the incubation mixture. In a similar manner, 4-fluorochalconeoxide-senaitive binding of epoxystearic acid to rat soluble epoxide hydrolase could be demonstrated in rat liver cytosol. Under similar conditions, no covalent binding of [26-'JC]cholesterol-5a,6n-epoxide to microsomal proteins or solubilized fractions tenfold enriched in cholesterol epoxide hydrolase activity could be observed. Our data provide definitive proof for the formation of an enzyme-substrate-ester intermediate formed in the course of epoxide hydrolysis by microsomal epoxide hydrolase, show no formation of a covalent intermediate between cholesterol epoxide hydrolase and its substrate under the same conditions as those under which an intermediate was shown for both microsomal and soluble epoxide hydrolases and therefore indicate that the cholesterol epoxide hydrolase apparently does not act by a similar mechanism and is probably not structurally related to microsomal and soluble epoxide hydrolases.Keywords ; epoxide hydrolase ; mechanism ; a/b hydrolase fold ; cholesterol ; fatty acid metabolism.Epoxide hydrolases (EH) represent a group of ubiquitous enzymes with important functions in the detoxification of reactive intermediates, namely epoxides, that arise from a large variety of compounds during their metabolism. The two mammalian enzymes implicated in the metabolism of foreign compounds are microsomal EH (Oesch, 1973) and soluble EH (Ota and Hammock, 1980). Both enzymes have been cloned from a variety of species (Beetham et al., 1993;Grant et al., 1993;Jackson et al., 1987;Knehr et al., 1993;Porter et al., 1986;Wojtasek and Prestwich, 1996). A third enzyme, cholesterol EH, which is membrane bound similarly to inicrosomal EH but otherwise distinct from the latter (Oesch et al., 1984), is less well investigated. Its physiological function appears to be the conversion of 5n,6n-epoxycholestane-3P-o1 and SP,6D-epoxycholestane-3/!-ol, the two epoxides arising from cholesterol during, e.g. lipid peroxidation, to give the single product cholestane-3~,Scr,b/j-triol (Watabe et al., 1981).For a long time it was believed that EH convert their substrates by direct hydrolysis. The pioneering work of Hanzli...

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“…However, IS1358 from V. cholerae (15) exhibited a 54% nucleotide residue identity with PGIS2. Protein sequence database searches also revealed significant homology between the putative polypeptide encoded by PGIS2 and the putative transposase of IS1358 from V. cholerae (15), the protein encoded by A. salmonicida IS element ISAS1 (5), the predicted product of H-rpt from E. coli K-12 (16), and a hypothetical protein encoded by a long ORF downstream of the dhlA gene of X. autotrophicus GJ10 (9). The amino acid alignment indicated that these proteins are more conserved in the central region (Fig.…”

mentioning

confidence: 99%

“…In this study we identified a second endogenous IS element in P. gingivalis. The predicted protein encoded by PGIS2 exhibits a high degree of homology to the putative transposases of IS1358 and ISAS1 from V. cholerae and A. salmonicida, respectively, the predicted product of H-rpt from E. coli K-12 (16), and a hypothetical protein encoded by a long ORF downstream of the dhlA gene of X. autotrophicus GJ10 (9). The additional copy of PGIS2 in P. gingivalis Tn4351 transconjugant MSM-1 suggests that either transposition of the endogenous PGIS2 element occurred following transposition of Tn4351 or transposition of PGIS2 spontaneously occurred during laboratory passage.…”

mentioning

confidence: 99%

“…In this study, we have identified a second endogenous P. gingivalis IS element and have confirmed the transposition of this element within P. gingivalis. The new IS element, designated PGIS2, is predicted to code for a polypeptide with strong homology to the putative transposases of IS1358 and ISAS1 from Vibrio cholerae and Aeromonas salmonicida, respectively (5, 15), the predicted product of H-rpt from Escherichia coli K-12 (16), and a hypothetical protein encoded by a long open reading frame (ORF) downstream of the dhlA gene of Xanthobacter autotrophicus GJ10 (9).…”

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confidence: 99%

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Identification of a second endogenous Porphyromonas gingivalis insertion element

1997

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In this study a second endogenous Porphyromonas gingivalis insertion element (IS element) that is capable of transposition within P. gingivalis was identified. Nucleotide sequence analysis of the Tn4351 insertion site in a P. gingivalis Tn4351-generated transconjugant showed that a complete copy of the previously unidentified IS element, designated PGIS2, had inserted into IS4351 R in Tn4351. PGIS2 is 1,207 bp in length with 19-bp imperfect terminal inverted repeats, and insertion resulted in a duplicated 10-bp target sequence. Results of Southern hybridization of chromosomal DNA isolated from several P. gingivalis strains with a PGIS2-specific probe demonstrated that the number of copies of PGIS2 per genome varies among different P. gingivalis strains. Computer analysis of the putative polypeptide encoded by PGIS2 revealed strong homologies to the products encoded by IS1358 from Vibrio cholerae, ISAS1 from Aeromonas salmonicida, and H-rpt in Escherichia coli K-12.Insertion elements (IS elements) are discrete genetic sequences capable of transposition to new locations within the prokaryotic chromosome, its bacteriophages, or its plasmids. These elements, which vary in size from 0.7 to 7.1 kilobase pairs (kb), contain little or no genetic information beyond that required for transposition. The terminal inverted repeats and duplicated target sequences are characteristic features for most IS elements. In spite of its relatively low frequency, transposition of IS elements is essential for their propagation and survival in a bacterial population (1). Transposition of IS elements also results in a number of genetic effects, including disruption of gene function, polarity effects, and activation of nearby genes or DNA rearrangements, all of which may contribute to the genetic diversity of a bacterial population (2).Porphyromonas gingivalis, an obligately anaerobic gram-negative cocobacillus, is an important pathogen in human periodontal disease. However, genetic analysis of P. gingivalis has been slow due to the lack of naturally occurring plasmids, bacteriophages, and efficient genetic transformation systems. Genco et al. (4) reported previously on the development of a transpositional mutagenesis system for P. gingivalis which uses Bacteroides fragilis transposon Tn4351. The high frequency of transposition, together with the observed stability of the insertion, indicated that Tn4351 mutagenesis would be a valuable tool for examining a variety of mutations in P. gingivalis. However, further characterization of P. gingivalis Tn4351 transconjugants indicated that Tn4351 had inserted 60 bp upstream from endogenous P. gingivalis IS element IS1126 (10). In addition, two additional copies of IS1126 were found in transconjugants compared to the wild-type strain, indicating that IS1126 was capable of mobilization in P. gingivalis (14). In this study, we have identified a second endogenous P. gingivalis IS element and have confirmed the transposition of this element within P. gingivalis. The new IS element, designated PGIS2, is...

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Cloning of 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression and sequencing of the dhlA gene

Cited by 215 publications

References 34 publications

Repositioning the Catalytic Triad Aspartic Acid of Haloalkane Dehalogenase: Effects on Stability, Kinetics, and Structure

Repositioning the Catalytic Triad Aspartic Acid of Haloalkane Dehalogenase: Effects on Stability, Kinetics, and Structure

Visualization of a Covalent Intermediate between Microsomal Epoxide Hydrolase, but not Cholesterol Epoxide Hydrolase, and their Substrates

Identification of a second endogenous Porphyromonas gingivalis insertion element

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