Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An experiment was conducted with growing rats to investigate the effects of feeding excessive specific L-amino acids for 8 days on serum and tissue cholesterol, alpha-tocopherol, ascorbic acid, and copper, and on liver microsomal cytochrome P-450. To a 10% casein diet were added 4% L-methionine, 5% L-cystine, 5% L-histidine, 5% L-threonine, 5% L-tryptophan, 5% L-phenylalanine, 5% L-tyrosine, 6% L-valine, 7% L-isoleucine, 7% L-lysine, or 8% L-leucine. Excessive cystine and histidine increased serum cholesterol and alpha-tocopherol. Excessive cystine and methionine increased liver and kidney alpha-tocopherol and ascorbic acid. Excessive tyrosine and phenylalanine caused a marked increase in serum copper and ceruloplasmin activity, whereas excessive cystine, methionine, and histidine caused a decrease in the ceruloplasmin activity. Excessive histidine increased liver cytochrome P-450, whereas excessive tyrosine markedly decreased liver cytochrome P-450.
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PMID:Effects of dietary excess amino acids on the concentrations of cholesterol, alpha-tocopherol, ascorbic acid, and copper in serum and tissues of rats. 209 20

The present paper describes a protective role of L-tyrosine against aggregation of caeruloplasmin and haemoglobin therapeutic proteins during their sterilization by gamma-irradiation in the aqueous phase. Irradiation of proteins, known to induce their degradation in the presence of oxygen, generates aggregation under oxygen-free conditions. It was found that L-tyrosine present during irradiation in deoxygenated media prevents protein aggregation even at high doses (10 kGy), as asserted by SDS/PAGE and high-performance size-exclusion chromatography. The protective role of L-tyrosine, allowing the gamma-irradiation treatment of therapeutic proteins in solution without conformational alteration, is probably exerted by scavenging oxygen radicals produced by irradiation-induced water radiolysis. It was also found that haemoglobin had a greater stability than caeruloplasmin under gamma-irradiation treatment.
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PMID:L-tyrosine prevents aggregation of therapeutic proteins by gamma-irradiation. 1277 96

It was previously shown that protein aggregation induced by gamma-irradiation can be prevented by L-tyrosine, even when irradiation was done in solution at doses as high as 10 kGy. It is now reported that caeruloplasmin irradiated at low to moderate doses appears more resistant to trypsin-mediated proteolysis than native caeruloplasmin. Ceruloplasmin presents an irradiation-dose-dependent decrease of oxidase activity and a slight increase of ferroxidase activity at low irradiation doses (2 kGy), followed by a decrease at high doses (4-8 kGy). In all cases, the catalytic activities are higher when caeruloplasmin is irradiated under tyrosine protection. Irradiated caeruloplasmin in the presence of tyrosine preserves its oxidase and ferroxidase activities. Caeruloplasmin irradiated in solution at a dose of 2-3 kGy and higher, in the presence and absence of L-tyrosine, remained sterile during at least 8 weeks of storage at 4 degrees C, as evaluated by the plate-count-agar method for assessing total viable lactic acid bacteria content after incubation for 48 h at 30 degrees C.
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PMID:Caeruloplasmin sterilized by gamma-irradiation in the presence of L-tyrosine maintains structural and catalytic characteristics. 1277 98

Multi-copper oxidases (MCOs) are widely distributed in bacteria, where they are responsible for metal homeostasis, acquisition and oxidation. Using specific primers, yacK coding for MCO was amplified from different serotypes of Yersinia enterocolitica biovar 1A. Homology modeling of the protein followed by docking with five well-known substrates for different MCO's (viz., 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid [ABTS], syringaldazine, L-tyrosine, ammonium ferrous sulfate and guaiacol), lignin monomers (Coniferyl alcohol, p-coumaryl alcohol and sinapyl alcohol) and two inhibitors i.e., kojic acid and N-hydroxyglycine was done. The docking gave maximum GoldScore i.e., 91.93 and 72.64 with ammonium ferrous sulfate and ABTS, respectively. Similarly, docking with ICM gave -82.10 and -83.61 docking score, confirming the protein to be true laccase with ferroxidase activity. Further, validation with ammonium ferrous sulfate as substrate gave laccase activity of 0.36Units/L/min. Guaiacol, L-tyrosine, and lignin monomers showed good binding affinity with protein models with GoldScores of 35.89, 41.82, 40.41, 41.12 and 43.10, respectively. The sequence study of all the cloned Yack genes showed serotype specific clade in dendrogram. There was distinct discrimination in the ligand binding affinity of Y. enterocolitica laccase, among strains of same clonal groups, suggesting it as a tool for phylogenetic studies.
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PMID:Molecular modeling and docking of novel laccase from multiple serotype of Yersinia enterocolitica suggests differential and multiple substrate binding. 2483 34