Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

p-Nitrophenyl 3-diazopyruvate (DAPpNP) has been developed as a heterobifunctional cross-linking agent for synthesis of photoaffinity probes and photoactivatable cross-linking agents that are nucleophile specific. p-Nitrophenyl chloroglyoxylate is formed in high yield from oxalyl chloride and p-nitrophenol. Subsequent reaction with diazomethane produces DAPpNP in 50-60% overall yield. DAPpNP acylates primary and secondary amines to form 3-diazopyruvamides in high yields. 3-Diazopyruvamide derivatives have been formed from a wide variety of amines including aromatic amines, amino acids, and peptides. 3-Diazopyruvamides undergo photolysis and Wolff rearrangement at 300 nm to produce a ketene amide, which efficiently acylates nucleophilic species to form malonic acid amide derivatives. A family of photoactivatable 3-diazopyruvamide cross-linking agents was synthesized from amino acids. A cleavable, thiol-specific photoactivatable cross-linking agent was synthesized from cystamine. These reagents were caused to react with rabbit muscle aldolase to form mainly dimeric cross-linked species.
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PMID:p-Nitrophenyl 3-diazopyruvate and diazopyruvamides, a new family of photoactivatable cross-linking bioprobes. 279 3

1. Mesophyll and parenchyma-sheath chloroplasts of maize leaves were separated by density fractionation in non-aqueous media. 2. An investigation of the distribution of photosynthetic enzymes indicated that the mesophyll chloroplasts probably contain the entire leaf complement of pyruvate,P(i) dikinase, NADP-specific malate dehydrogenase, glycerate kinase and nitrite reductase and most of the adenylate kinase and pyrophosphatase. The fractionation pattern of phosphopyruvate carboxylase suggested that this enzyme may be associated with the bounding membrane of mesophyll chloroplasts. 3. Ribulose diphosphate carboxylase, ribose phosphate isomerase, phosphoribulokinase, fructose diphosphate aldolase, alkaline fructose diphosphatase and NADP-specific ;malic' enzyme appear to be wholly localized in the parenchyma-sheath chloroplasts. Phosphoglycerate kinase and NADP-specific glyceraldehyde phosphate dehydrogenase, on the other hand, are distributed approximately equally between the two types of chloroplast. 4. After exposure of illuminated leaves to (14)CO(2) for 25sec., labelled malate, aspartate and 3-phosphoglycerate had similar fractionation patterns, and a large proportion of each was isolated with mesophyll chloroplasts. Labelled fructose phosphates and ribulose phosphates were mainly isolated in fractions containing parenchyma-sheath chloroplasts, and dihydroxyacetone phosphate had a fractionation pattern intermediate between those of C(4) dicarboxylic acids and sugar phosphates. 6. These results indicate that the mesophyll and parenchyma-sheath chloroplasts have a co-operative function in the operation of the C(4)-dicarboxylic acid pathway. Possible routes for the transfer of carbon from C(4) dicarboxylic acids to sugars are discussed.
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PMID:Distribution of enzymes in mesophyll and parenchyma-sheath chloroplasts of maize leaves in relation to the C4-dicarboxylic acid pathway of photosynthesis. 430 27

The ability of rat liver zinc-thionein to donate its metal to the apo-enzymes of the zinc enzymes horse liver alcohol dehydrogenase, yeast aldolase, thermolysin, Escherichia coli alkaline phosphatase and bovine erythrocyte carbonic anhydrase was investigated. Zinc-thionein was as good as, or better than, ZnSO(4), Zn(CH(3)CO(2))(2) or Zn(NO(3))(2) in donating its zinc to these apo-enzymes. Apo-(alcohol dehydrogenase) could not be reactivated by zinc salts or by zinc-thionein. Incubation of the other apo-enzymes with near-saturating amounts of zinc as ZnSO(4), Zn(CH(3)CO(2))(2), Zn(NO(3))(2), or zinc-thionein resulted in reactivation of the apo-enzymes. With apo-aldolase zinc-thionein gave 100% reactivation within 30min. Reactivation by ZnSO(4) and Zn(CH(3)CO(2))(2) was complete and instantaneous. Zinc-thionein was somewhat better than Zn(NO(3))(2) in completely reactivating apo-thermolysin. With apo-(alkaline phosphatase) 43% reactivation was obtained with Zn(CH(3)CO(2))(2) and 18% with zinc-thionein. With apo-(carbonic anhydrase) zinc-thionein was better than ZnSO(4), Zn(CH(3)CO(2))(2) or Zn(NO(3))(2), with a maximal reactivation of 54%. That zinc was really being transferred from zinc-thionein to apo-(carbonic anhydrase) was shown by the fact that 2,6-pyridine dicarboxylic acid and 1,10-phenanthroline had minimal effects on the reactivation of apo-(carbonic anhydrase) when added after the incubation {[apo-(carbonic anhydrase)+zinc thionein]+chelator}, but inhibited reactivation when added before the incubation {apo-(carbonic anhydrase)+[zinc-thionein+chelator]}. These observations support the idea that zinc-thionein can function in zinc homeostasis as a reservoir of zinc, releasing the metal to zinc-requiring metalloenzymes according to need.
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PMID:Reactivation in vitro of zinc-requiring apo-enzymes by rat liver zinc-thionein. 677 58

Two new genes whose products are involved in biodegradation of the organic solvent tetralin were identified. These genes, designated thnE and thnF, are located downstream of the previously identified thnD gene and code for a hydratase and an aldolase, respectively. A sequence comparison of enzymes similar to ThnE showed the significant similarity of hydratases involved in biodegradation pathways to 4-oxalocrotonate decarboxylases and established four separate groups of related enzymes. Consistent with the sequence information, characterization of the reaction catalyzed by ThnE showed that it hydrated a 10-carbon dicarboxylic acid. The only reaction product detected was the enol tautomer, 2,4-dihydroxydec-2-ene-1,10-dioic acid. The aldolase ThnF showed significant similarity to aldolases involved in different catabolic pathways whose substrates are dihydroxylated dicarboxylic acids and which yield pyruvate and a semialdehyde. The reaction products of the aldol cleavage reaction catalyzed by ThnF were identified as pyruvate and the seven-carbon acid pimelic semialdehyde. ThnF and similar aldolases showed conservation of the active site residues identified by the crystal structure of 2-dehydro-3-deoxy-galactarate aldolase, a class II aldolase with a novel reaction mechanism, suggesting that these similar enzymes are class II aldolases. In contrast, ThnF did not show similarity to 4-hydroxy-2-oxovalerate aldolases of other biodegradation pathways, which are significantly larger and apparently are class I aldolases.
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PMID:Identification of a hydratase and a class II aldolase involved in biodegradation of the organic solvent tetralin. 1232 29

Mycobacterium sp. strains CP1, CP2, CFt2 and CFt6 were isolated from creosote-contaminated soil due to their ability to grow in pyrene (CP1 and CP2) or fluoranthene (CFt2 and CFt6). All these strains utilized fluoranthene as a sole source of carbon and energy. Strain CP1 exhibited the best growth, with a cellular assimilation of fluoranthene carbon of approximately 45%. Identification of the metabolites accumulated during growth in fluoranthene, the kinetics of metabolites, and metabolite feeding studies, indicated that all these isolates oxidized fluoranthene by the following two routes: the first involves dioxygenation at C-1 and C-2, meta cleavage, and a 2-carbon fragment excision to produce 9-fluorenone-1-carboxylic acid. An angular dioxygenation of the latter yields cis-1,9a-dihydroxy-1-hydrofluorene-9-one-8-carboxylic acid, which is further degraded via 8-hydroxy-3,4-benzocoumarin-1-carboxylic acid, benzene-1,2,3-tricarboxylic acid, and phthalate; the second route involves dioxygenation at C-2 and C-3 and ortho cleavage to give Z-9-carboxymethylenefluorene-1-carboxylic acid. In addition, the pyrene-degrading strains CP1 and CP2 possess a third route initiated by dioxygenation at positions C-7 and C-8, which--following meta cleavage, an aldolase reaction, and a C(1)-fragment excision--yields acenaphthenone. Monooxygenation of this ketone to the corresponding quinone, and its subsequent hydrolysis, produces naphthalene-1,8-dicarboxylic acid. The results obtained in this study not only complete and confirm the three fluoranthene degradation routes previously proposed for the pyrene-degrading strain Mycobacterium sp. AP1, but also suggest that such routes represent general microbial processes for environmental fluoranthene removal.
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PMID:Metabolism of fluoranthene by mycobacterial strains isolated by their ability to grow in fluoranthene or pyrene. 1613 98

Pentachlorophenol is the most toxic and recalcitrant chlorophenol because both aspects are directly proportional to the halogenation degree. Biological and abiotic pentachlorophenol degradation generates p-chloranil, which in neutral to lightly alkaline environmental conditions is hydrolyzed to chloranilic acid that present a violet-reddish coloration in aqueous solution. Several genes of the degradation pathway, cadR-cadCDX, as well as other uncharacterized genes (ORF5 and 6), were isolated from a chloranilic acid degrading bacterium, Pseudomonas putida strain TQ07. The disruption by random mutagenesis of the cadR and cadC genes in TQ07 resulted in a growth deficiency in the presence of chloranilic acid, indicating that these genes are essential for TQ07 growth with chloranilic acid as the sole carbon source. Complementation assays demonstrated that a transposon insertion in mutant CAD82 (cadC) had a polar effect on other genes contained in cosmid pLG3562. These results suggest that at least one of these genes, cadD and cadX, also takes part in chloranilic acid degradation. Based on molecular modeling and function prediction, we strongly suggest that CadC is a pyrone dicarboxylic acid hydrolase and CadD is an aldolase enzyme like dihydrodipicolinate synthase. The results of this study allowed us to propose a novel pathway that offers hypotheses on chloranilic acid degradation (an abiotic by-product of pentachlorophenol) by means of a very clear phenotype that is narrowly related to the capability of Pseudomonas putida strain TQ07 to degrade this benzoquinone.
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PMID:Molecular characterization of chloranilic acid degradation in Pseudomonas putida TQ07. 2220 61

Glyoxylate detoxification is an important function of human peroxisomes. Glyoxylate is a highly reactive molecule, generated in the intermediary metabolism of glycine, hydroxyproline and glycolate mainly. Glyoxylate accumulation in the cytosol is readily transformed by lactate dehydrogenase into oxalate, a dicarboxylic acid that cannot be metabolized by mammals and forms tissue-damaging calcium oxalate crystals. Alanine-glyoxylate aminotransferase, a peroxisomal enzyme in humans, converts glyoxylate into glycine, playing a central role in glyoxylate detoxification. Cytosolic and mitochondrial glyoxylate reductase also contributes to limit oxalate production from glyoxylate. Mitochondrial hydroxyoxoglutarate aldolase is an important enzyme of hydroxyproline metabolism. Genetic defect of any of these enzymes of glyoxylate metabolism results in primary hyperoxalurias, severe human diseases in which toxic levels of oxalate are produced by the liver, resulting in progressive renal damage. Significant advances in the pathophysiology of primary hyperoxalurias have led to better diagnosis and treatment of these patients, but current treatment relies mainly on organ transplantation. It is reasonable to expect that recent advances in the understanding of the molecular mechanisms of disease will result into better targeted therapeutic options in the future.
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PMID:Primary hyperoxalurias: disorders of glyoxylate detoxification. 2244 32