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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cyclic version of the Entner-Doudoroff pathway is used by Pseudomonas aeruginosa to metabolize carbohydrates. Genes encoding the enzymes that catabolize intracellular glucose to pyruvate and glyceraldehyde 3-phosphate are coordinately regulated, clustered at 39 min on the chromosome, and collectively form the hex regulon. Within the hex cluster is an open reading frame (ORF) with homology to the devB/SOL family of unidentified proteins. This ORF encodes a protein of either 243 or 238 amino acids; it overlaps the 5' end of zwf (encodes glucose-6-phosphate dehydrogenase) and is followed immediately by eda (encodes the Entner-Doudoroff aldolase). The devB/SOL homolog was inactivated in P. aeruginosa PAO1 by recombination with a suicide plasmid containing an interrupted copy of the gene, creating mutant strain PAO8029. PAO8029 grows at 9% of the wild-type rate using mannitol as the carbon source and at 50% of the wild-type rate using gluconate as the carbon source. Cell extracts of PAO8029 were specifically deficient in 6-phosphogluconolactonase (Pgl) activity. The cloned devB/SOL homolog complemented PAO8029 to restore normal growth on mannitol and gluconate and restored Pgl activity. Hence, we have identified this gene as pgl and propose that the devB/SOL family members encode 6-phosphogluconolactonases. Interestingly, three eukaryotic glucose-6-phosphate dehydrogenase (G6PDH) isozymes, from human, rabbit, and Plasmodium falciparum, contain Pgl domains, suggesting that the sequential reactions of G6PDH and Pgl are incorporated in a single protein. 6-Phosphogluconolactonase activity is induced in P. aeruginosa PAO1 by growth on mannitol and repressed by growth on succinate, and it is expressed constitutively in P. aeruginosa PAO8026 (hexR). Taken together, these results establish that Pgl is an essential enzyme of the cyclic Entner-Doudoroff pathway encoded by pgl, a structural gene of the hex regulon.
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PMID:The Pseudomonas aeruginosa devB/SOL homolog, pgl, is a member of the hex regulon and encodes 6-phosphogluconolactonase. 1086 70

Syringolide 2, an elicitor of the bacterial plant pathogen Pseudomonas syringae pv. tomato which triggers a hypersensitive defense response in resistant soybean plants, has been synthesized in five steps via a fructose 1,6-diphosphate aldolase reaction.
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PMID:Chemoenzymatic synthesis of the microbial elicitor (-)-syringolide via a fructose 1,6-diphosphate aldolase-catalyzed condensation reaction. 1095 54

The gene loci ech, encoding enoyl-CoA hydratase/aldolase, and fcs, encoding an unusual feruloyl-CoA synthetase, which are involved in the bioconversion of ferulic acid to vanillin by the gram-positive bacterium Amycolatopsis sp. strain HR167, were localized on a 4,000 bp PstI fragment (P40). The nucleotide sequence of P40 was determined, revealing open reading frames of 864 bp and 1,476 bp, representing ech and fcs, respectively. The deduced amino acid sequences of ech exhibited 62% amino acid identity to the enoyl-CoA hydratase/aldolase from Pseudomonas sp. strain HR199 and the enoyl-CoA hydratase/lyase from P. fluorescens strain AN103. The deduced amino acid sequences of fcs exhibited up to 37% amino acid identity to long-chain fatty acid coenzymeA ligases but no significant similarity to the feruloyl-CoA synthetase of Pseudomonas sp. strain HR199. Fragment P40 was cloned in pBluescript SK- and fcs and ech were expressed in Escherichia coli. Recombinant strains were able to transform ferulic acid to vanillin. In crude extracts of these recombinant strains, feruloyl-CoA synthetase and enoyl-CoA hydratase/aldolase activities were detected by photometric assay and high-performance liquid chromatography. The obtained data suggest that ferulic acid degradation in the gram-positive Amycolatopsis sp. strain HR167 proceeds via a pathway similar to that recently described for the gram-negative P. fluorescens strain AN103 and Pseudomonas sp. strain HR199.
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PMID:Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin. 1115 72

The final two steps of the meta-cleavage pathway for catechol degradation in Pseudomonas sp. strain CF600 involve the conversion of 4-hydroxy-2-ketovalerate to pyruvate and acetyl coenzyme A by the enzymes 4-hydroxy-2-ketovalerate aldolase and NAD(+)-dependent acylating aldehyde dehydrogenase. Biochemical studies indicate that these two enzymes comprise a bifunctional heterodimer (DmpFG, molecular mass 71 kDa) and suggest that the product of the aldolase reaction is transferred to the dehydrogenase active site via a channeling mechanism. Crystals of the DmpFG complex grow in multiple fan-like clusters of thin plates by the hanging-drop method and are improved by streak-seeding. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 102.0, b = 140.7, c = 191.3 A, and diffract to 2.1 A resolution. The asymmetric unit contains four DmpFG heterodimers. Heavy-atom derivative screening identified three isomorphous derivatives.
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PMID:Crystallization and preliminary X-ray analysis of dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase--aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600. 1126 89

Sphingomonas xenophaga BN6 was isolated from the river Elbe as a member of a multispecies bacterial culture which mineralized 6-aminonaphthalene-2-sulfonate. Pure cultures of strain BN6 converted a wide range of amino- and hydroxynaphthalene-2-sulfonates via a catabolic pathway similar to that described for the metabolism of naphthalene to salicylate by Pseudomonas putida NAH7 or Pseudomonas sp NCIB 9816. In contrast to the naphthalene-degrading pseudomonads, S. xenophaga BN6 only partially degraded the naphthalenesulfonates and excreted the resulting amino- and hydroxysalicylates in almost stoichiometric amounts. Enzymes that take part in the degradative pathway of the naphthalenesulfonates by strain BN6 were purified, characterized and compared with the isofunctional enzymes from the naphthalene-degrading pseudomonads. According to the enzyme structures and the catalytic constants, no fundamental differences were found between the 1,2-dihydroxynaphthalene dioxygenase or the 2'-hydroxybenzalpyruvate aldolase from strain BN6 and the isofunctional enzymes from the naphthalene-degrading pseudomonads. The limited available sequence information about the enzymes from strain BN6 suggests that they show about 40-60% sequence identity to the isofunctional enzymes from the pseudomonads. In addition to the gene for the 1,2-dihydroxynaphthalene dioxygenase, the genes for two other extradiol dioxygenases were cloned and sequenced from strain BN6 and the corresponding gene products were studied. S. xenophaga BN6 has also been used as a model organism to study the mechanism of the non-specific reduction of azo dyes under anaerobic conditions and to establish combined anaerobic/aerobic treatment systems for the degradation of sulfonated azo dyes. Furthermore, the degradation of substituted naphthalenesulfonates by mixed cultures containing strain BN6 was studied in continuous cultures and was described by mathematical models.
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PMID:Degradation of substituted naphthalenesulfonic acids by Sphingomonas xenophaga BN6. 1142 60

The gene loci fcs and ech, encoding feruloyl-CoA synthetase and enoyl-CoA hydratase/aldolase, respectively, are involved in the ferulic acid catabolism in Delftia acidovorans. The amino acid sequence deduced from ech exhibited 51% identity to the enoyl-CoA hydratase/aldolase from Pseudomonas sp. strain HR199, indicating that the enzyme from D. acidovorans represents a new lineage of this protein. The genes fcs and ech were expressed in Escherichia coli enabling the recombinant strain to transform ferulic acid to vanillin as revealed by photometric and HPLC analysis. An fcs deficient mutant of D. acidovorans was unable to grow on ferulic acid. The obtained data suggest that in contrast to a previous publication the biotechnologically interesting direct non-oxidative deacetylation mechanism of ferulic acid cleavage is not realized in D. acidovorans. Instead, ferulic acid degradation in D. acidovorans proceeds via a coenzyme A-dependent non-beta-oxidative pathway.
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PMID:The coenzyme A-dependent, non-beta-oxidation pathway and not direct deacetylation is the major route for ferulic acid degradation in Delftia acidovorans. 1172 9

A 3.9-kb fragment of the genome of Pseudomonas putida H, containing the complete zwf-pgl-eda-operon, encoding glucose 6-phosphate dehydrogenase, 6-phosphogluconolactonase and 2-keto-3-deoxy-6-phosphogluconate-aldolase, respectively, and part of the divergently transcribed regulatory gene, hexR, was cloned and analyzed. The nucleotide sequences of these genes showed high similarities to the corresponding DNA sequences of P. putida KT2440 and also to sequences of Pseudomonas aeruginosa PAO1. Derivatives of strains H and KT2440, containing transcriptional lacZ fusions to P(zwf) were generated and used to study the expression of these operons. In both strains, this operon was induced by carbohydrates such as glucose, gluconate, fructose and glycerol. The transcription rate of the zwf-pgl-eda-operon was found to be about three times higher in the KT2440 background than in strain H. In both strains the induction of the zwf-pgl-eda-operon by carbohydrates during growth on carboxylic acids was not affected by carbon catabolite repression.
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PMID:Analysis of the zwf-pgl-eda-operon in Pseudomonas putida strains H and KT2440. 1239 6

The protocatechuate (PCA) 4,5-cleavage pathway is the essential metabolic route for degradation of low-molecular-weight products derived from lignin by Sphingomonas paucimobilis SYK-6. In the 10.5-kb EcoRI fragment carrying the genes for PCA 4,5-dioxygenase (ligAB), 2-pyrone-4,6-dicarboxylate hydrolase (ligI), 4-oxalomesaconate hydratase (ligJ), and a part of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (ligC), we found the ligK gene, which encodes 4-carboxy-4-hydroxy-2-oxoadipate (CHA) aldolase. The ligK gene was located 1,183 bp upstream of ligI and transcribed in the same direction as ligI. We also found the ligR gene encoding a LysR-type transcriptional activator, which was located 174 bp upstream of ligK. The ligK gene consists of a 684-bp open reading frame encoding a polypeptide with a molecular mass of 24,131 Da. The deduced amino acid sequence of ligK showed 57 to 88% identity with those of the corresponding genes recently reported in Sphingomonas sp. strain LB126, Comamonas testosteroni BR6020, Arthrobacter keyseri 12B, and Pseudomonas ochraceae NGJ1. The ligK gene was expressed in Escherichia coli, and the gene product (LigK) was purified to near homogeneity. Electrospray-ionization mass spectrometry indicated that LigK catalyzes not only the conversion of CHA to pyruvate and oxaloacetate but also that of oxaloacetate to pyruvate and CO(2). LigK is a hexamer, and its isoelectric point is 5.1. The K(m) for CHA and oxaloacetate are 11.2 and 136 micro M, respectively. Inactivation of ligK in S. paucimobilis SYK-6 resulted in the growth deficiency of vanillate and syringate, indicating that ligK encodes the essential CHA aldolase for catabolism of these compounds. Reverse transcription-PCR analysis revealed that the PCA 4,5-cleavage pathway genes of S. paucimobilis SYK-6 consisted of four transcriptional units, including the ligK-orf1-ligI-lsdA cluster, the ligJAB cluster, and the monocistronic ligR and ligC genes.
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PMID:Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6. 1248 39

Pseudomonas putida KT2440 is a physiologically extremely versatile non-pathogenic bacterium that is applied as a "biosafety strain" in biotechnological processes, as authorized by the USA National Institute of Health. Analysis of the P. putida KT2440 whole-genome sequence revealed the genetic organization of the genes fcs, ech, and vdh, which are essential for ferulic acid conversion to vanillic acid via vanillin. To confirm the physiological function of these structural genes as feruloyl-CoA synthetase (Fcs), enoyl-CoA hydratase/aldolase (Ech), and vanillin dehydrogenase (Vdh), respectively, they were cloned and expressed in Escherichia coli. Recombinant strains harboring fcs and ech were able to transform ferulic acid to vanillin. The enzyme activities of Fcs and Vdh were determined in protein extracts of these cells. The essential involvement of fcs, ech and vdh in the catabolism of ferulic acid in P. putida KT2440 was proven by separately inactivating each gene by insertion of Omega-elements. The corresponding mutant strains KT2440 fcsOmegaKm, KT2440 echOmegaKm, and KT2440 vdhOmegaKm were not able to grow on ferulic acid. The potential application of P. putida KT2440 and the mutant strains in biotechnological vanillin production process is discussed.
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PMID:Functional analyses of genes involved in the metabolism of ferulic acid in Pseudomonas putida KT2440. 1276 69

Creation of the Department of Biochemistry of Microorganisms at the Institute of Microbiology and Virology of the Academy of Sciences of Ukrainian SSR in the 30's of the last century was determined by a necessity of profound investigation of vital activity biochemism of microorganisms from various systematic groups which were studied in microbiological department of the Institute. Such complexity can explain certain diversity of the Department research at initial stages of its existence. The research of saccharose transformation into dextran Leuconostoc mesenteroides, when production solutions become slingy at sugar-refinaries, was one of the first most significant works of the Department. The enzyme saccharose-glycosyl-transferase performing this process was described for the first time. A cycle of works on the study of enzymes splitting lactose in milk under the effect of Streptococcus lactis has been carried out. Complex investigation of a number of proteins, polysaccharides, enzymes in enterobacteria has shown that the blocking of the enzyme aldolase is one of the reasons of alkali formation. A method has been developed for isolation of arenarin, antibiotic of plant origin, from sandy everlasting, the nature of its acting basis has been established. Nufarin, an active antibiotic, was isolated from the roots of white water lily when studying nitrogen fixation processes, special attention was given to interaction of hydrogenase and enzymes, taking part in nitrogen fixation, to the effect of ATP on these processes, ways of its synthesis, localization of ATPase in the cell membranes. Works on the study of lypopolysaccharides and polysaccharides of Gram-negative enterobacteria, bacteria of Pseudomonas genus were started with the purpose to use the obtained data to specify systematic propositions of the investigated microorganisms. Further on these works became the basis of thematic department. There are numerous reviews dedicated to their development.
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PMID:[Department of Biochemistry of Microorganisms--start of the path (1951-1973)]. 1277 2


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