Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:5.3.3.4 (muconolactone isomerase)
29 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recurring patterns of primary structure have been observed in enzymes that mediate sequential metabolic reactions in bacteria. The enzymes, muconolactone Delta-isomerase [(+)-4-hydroxy-4-carboxymethylisocrotonolactone Delta(2)-Delta(3)-isomerase, EC 5.3.3.4] and beta-ketoadipate enol-lactone hydrolase [4-carboxymethylbut-3-enolide(1,4)enol-lactone-hydrolase, EC 3.1.1.24], have been coselected in bacterial populations because the isomerase can confer no nutritional advantage in the absence of the hydrolase. Similar amino acid sequences recur within the structure of the isomerase, and the amino-terminal amino acid sequence of the isomerase from Pseudomonas putida appears to be evolutionarily homologous with the corresponding sequence of a beta-ketoadipate enol-lactone hydrolase from Acinetobacter calcoaceticus. One interpretation of the sequence repetitions is that they reflect tandem duplication mutations that took place early in the evolution of the proteins. According to this view, the mutations caused elongation of structural genes and the creation of duplicated genes as the metabolic pathways evolved. A review of the sequence data calls attention to a different hypothesis: repeated amino acid sequences were introduced in the course of the proteins' evolution by substitution of copies of DNA sequences into structural genes. Our observations are interpreted on the basis of a model proposing genetic exchange between misaligned DNA sequences. The model predicts that misalignments in one chromosomal region can influence the nature of mutations in another region. Thus, as often has been observed, the mutability of a base pair will be determined by its location in a DNA sequence. Furthermore, the intrachromosomal recombination of DNA sequences may account for complex genetic modifications that occur as new pathways evolve. The model provides an interpretation of an apparent paradox, the rapid creation of new metabolic traits by bacterial genomes that are remarkably resistant to genetic drift.
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PMID:Origins of metabolic diversity: evolutionary divergence by sequence repetition. 29 Oct 59

Muconolactone isomerase is shown to be resistant to proteolytic cleavage by trypsin. Cyanogen bromide cleavage at the methionine residues of the polypeptide is at least 95% complete. Six cyanogen bromide fragments are separated on DEAE-cellulose. One fragment is shown by amino acid analysis and carboxyl-terminal analysis to be an incomplete cleavage product. The five remaining fragments represent the entire polypeptide and have been ordered with respect to the entire muconolactone isomerase sequence. Approximately 50% of the polypeptide sequence could be determined from these fragments by the dansyl-Edman technique. The possible evolutionarily homologous origins of muconolactone isomerase and two analogous isomerases, carboxymuconolactone decarboxylase and sigma5-3-ketosteroid isomerase, are discussed.
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PMID:Purification and partial amino acid sequence of the cyanogen bromide fragments of muconolactone isomerase from Pseudomonas putida. 90 11

The catB and catC genes encode cis,cis-muconate lactonizing enzyme I (EC 5.5.1.1) and muconolactone isomerase (EC 5.3.3.4), respectively. These enzymes are required for the dissimilation of benzoate to beta-ketoadipate by Pseudomonas putida and are under coordinate transcriptional regulation. By deletion analysis and the use of pKT240 as a promoter probe vector, we located a single promoter region for the catBC operon upstream of catB. RNA-DNA hybridization studies, together with reverse transcriptase mapping, demonstrated that this promoter must be activated in the presence of an inducer molecule for effective transcription of the operon. In addition, the transcription initiation site was located 64 base pairs upstream of the catB initiation codon, and sequences upstream of -43 were required for promoter function. The catBC promoter was compared with other positively regulated procaryotic promoters to identify possible consensus sequences.
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PMID:Transcriptional regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida. 244 20

Pseudomonas putida utilizes the catBC operon, which encodes cis,cis-muconate lactonizing enzyme I (MLEI; EC 5.5.1.1) and muconolactone isomerase (MI; EC 5.3.3.4), for growth on benzoate as a sole carbon source. This operon is positively regulated, and the promoter is located 64 bp upstream of the catB translational start site. Using site-specific mutagenesis, we identified nucleotides that influenced the induction of this promoter. Promoter activity was monitored with the promoter probe vector pKT240. Transcription of mRNA from mutant promoters was determined by primer extension mapping. Comparison of the initiation start site of mutant promoters with that of the wild-type promoter identified a single functional promoter.
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PMID:Identification of nucleotides critical for activity of the Pseudomonas putida catBC promoter. 277 16

The crystal structure of muconolactone isomerase from Pseudomonas putida, a unique molecule with ten 96 amino acid subunits and 5-fold, and 2-fold symmetries, has been solved at 3.3 A resolution. The non-crystallographic symmetries were used to refine the initial single isomorphous replacement phases and produce an interpretable 10-fold averaged map. The backbone trace is complete and confirmed by the amino acid sequence fit. Each subunit is composed of a body with two alpha-helices and an antiparallel twisted beta-sheet of four strands, and an extended arm. The helices and the sheet fold to form a two-layered structure with an enclosed hydrophobic core and a partially formed putative active site pocket. The C-terminal arm of another subunit related by a local dyad symmetry extends over the core to complete this pocket. The decameric protein is almost spherical, with the helices forming the external coat. There is a large hydrophilic cavity in the center with open ends along the 5-fold axis. Molecular interactions between subunits are extensive. Each subunit contacts four neighbors and loses nearly 40% of its solvent contact area on oligomerization.
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PMID:Crystal structure of muconolactone isomerase at 3.3 A resolution. 292 18

This report describes the isolation and preliminary characterization of a 5.0-kilobase-pair (kbp) EcoRI DNA restriction fragment carrying the catBCDE genes from Acinetobacter calcoaceticus. The respective genes encode enzymes that catalyze four consecutive reactions in the catechol branch of the beta-ketoadipate pathway: catB, muconate lactonizing enzyme (EC 5.5.1.1); catC, muconolactone isomerase (EC 5.3.3.4); catD, beta-ketoadipate enol-lactone hydrolase (EC 3.1.1.24); and catE, beta-ketoadipate succinyl-coenzyme A transferase (EC 2.8.3.6). In A. calcoaceticus, pcaDE genes encode products with the same enzyme activities as those encoded by the respective catDE genes. In Pseudomonas putida, the requirements for both catDE and pcaDE genes are met by a single set of genes, designated pcaDE. A P. putida mutant with a dysfunctional pcaE gene was used to select a recombinant pKT230 plasmid carrying the 5.0-kbp EcoRI restriction fragment containing the A. calcoaceticus catE structural gene. The recombinant plasmid, pAN1, complemented P. putida mutants with lesions in catB, catC, pcaD, and pcaE genes; the complemented activities were expressed constitutively in the recombinant P. putida strains. After introduction into Escherichia coli, the pAN1 plasmid expressed the activities constitutively but at much lower levels that those found in the P. putida transformants or in fully induced cultures of A. calcoaceticus or P. putida. When placed under the control of a lac promoter on a recombinant pUC13 plasmid in E. coli, the A. calcoaceticus restriction fragment expressed catBCDE activities at levels severalfold higher than those found in fully induced cultures of A. calcoaceticus. Thus there is no translational barrier to expression of the A. calcoaceticus genes at high levels in E. coli. The genetic origin of the cloned catBCDE genes was demonstrated by the fact that the 5.0-kbp EcoRI restriction fragment hybridized with a corresponding fragment from wild-type A. calcoaceticus DNA. This fragment was missing in DNA from an A. calcoaceticus mutant in which the cat genes had been removed by deletion. The properties of the cloned fragment demonstrate physical linkage of the catBCDE genes and suggest that they are coordinately transcribed.
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PMID:Cloning and expression of Acinetobacter calcoaceticus catBCDE genes in Pseudomonas putida and Escherichia coli. 300 31

A 9.9-kilobase (kb) BamHI restriction endonuclease fragment encoding the catA and catBC gene clusters was selected from a gene bank of the Pseudomonas aeruginosa PAO1c chromosome. The catA, catB, and catC genes encode enzymes that catalyze consecutive reactions in the catechol branch of the beta-ketoadipate pathway: catA, catechol-1,2-dioxygenase (EC 1.13.11.1); catB, muconate lactonizing enzyme (EC 5.5.1.1); and catC, muconolactone isomerase (EC 5.3.3.4). A recombinant plasmid, pRO1783, which contains the 9.9-kb BamHI restriction fragment complemented P. aeruginosa mutants with lesions in the catA, catB, or catC gene; however, this fragment of chromosomal DNA did not contain any other catabolic genes which had been placed near the catA or catBC cluster based on cotransducibility of the loci. Restriction mapping, deletion subcloning, and complementation analysis showed that the order of the genes on the cloned chromosomal DNA fragment is catA, catB, catC. The catBC genes are tightly linked and are transcribed from a single promoter that is on the 5' side of the catB gene. The catA gene is approximately 3 kb from the catBC genes. The cloned P. aeruginosa catA, catB, and catC genes were expressed at basal levels in blocked mutants of Pseudomonas putida and did not exhibit an inducible response. These observations suggest positive regulation of the P. aeruginosa catA and catBC cluster, the absence of a positive regulatory element from pRO1783, and the inability of the P. putida regulatory gene product to induce expression of the P. aeruginosa catA, catB, and catC genes.
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PMID:Cloning and expression of the catA and catBC gene clusters from Pseudomonas aeruginosa PAO. 313 26

A number of spontaneous mutant strains of Pseudomonas putida, obtained by repeated selection for inability to grow with cis,cis-muconate, have been shown to carry deletions in catB, the structural gene for muconate lactonizing enzyme. These strains have been employed for deletion mapping of the genetic region containing catB and catC (the structural gene for muconolactone isomerase, the synthesis of which is coordinate with that of muconate lactonizing enzyme). All deletions that overlap mutant sites located on the left side of the genetic map, as well as the point mutations in that region, lead to a pleiotropic loss of both catB and catC activities. We propose that this region to the left of catB has a regulatory function. Although the details of regulation at the molecular level are unclear, our data indicate that catB and catC may well be controlled by a mechanism unlike any yet described by workers on enteric bacteria.
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PMID:Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: deletion mapping of cat mutations. 462 87

Crystalline preparations of muconate lactonizing enzyme and muconolactone isomerase, two inducible enzymes that catalyze successive steps in the catechol branch of the beta-ketoadipate pathway, were used to prepare antisera. Both enzymes were isolated from a strain of Pseudomonas putida biotype A. The antisera did not cross-react with enzymes of the same bacterial strain that catalyze the chemically analogous steps in the protocatechuate branch of the beta-ketoadipate pathway, carboxymuconate lactonizing enzyme and carboxymuconolactone decarboxylase. The antisera gave heterologous cross-reactions of varying intensities with the muconate lactonizing enzymes and muconolactone isomerases of P. putida biotype B, P. aeruginosa, P. stutzeri, and all biotypes of P. fluorescens, but did not cross-react with the isofunctional enzymes of P. acidovorans, of P. multivorans, and of two bacterial species that belong to other genera. The evolutionary and taxonomic implications of the findings are discussed.
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PMID:Comparative immunological studies of two Pseudomonas enzymes. 498 59

Several mutant strains of Pseudomonas putida, selected on the basis of their inability to grow at the expense of benzoate, have been shown to be unable to form inducibly both muconate lactonizing enzyme and muconolactone isomerase. A secondary mutant strain derived from one of these pleiotropically negative strains forms these two enzymes and, in addition, catechol oxygenase in the absence of inducer. This constitutive mutant strain was used as a donor in transductionally mediated two-point crosses to determine the order of point mutations within the structural genes for muconate lactonizing enzyme and muconolactone isomerase (the catB and catC genes, respectively). The gene order conformed precisely with the one that has been established by deletion mapping.
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PMID:Genetic control of enzyme induction in the -ketoadipate pathway of Pseudomonas putida: two-point crosses with a regulatory mutant strain. 505 53


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