Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4) on phytate dephosphorylation. Pepsin (EC 3.4.23.1) and pancreatin digestion periods were preceded by a 30 min pre-incubation at pH 5.25 to simulate digestion in the crop of poultry. Pancreatin digestion was carried out in dialysis tubing, with a ratio of about 1:25 (v/v) between the digesta and dialysing medium, to simulate gradient absorption from the duodenum. The feed:water ratio was kept within physiological limits and a constant proportion of feed weight to digestive enzymes was maintained. There was a linear response to increasing dosages of phytase up to 1000 phytase units (FTU)/kg feed, and to increasing phosphate concentration in feeds. In vivo validation was performed with growing turkeys (1-3 weeks) fed on diets containing 12 g Ca/kg and 0, 500 or 1000 FTU phytase/kg in a factorial arrangement with 0, 1, 2 or 3 g supplemental phosphate/kg (from KH2PO4). After a simple transformation (variable/in vitro P = f (in vitro P)), amounts of P hydrolysed from feed samples by in vitro digestions correlated with 3-week body-weight gain (R 0.986, P < 0.0001), toe ash (R 0.952, P < 0.0001), feed intake (R 0.994, P < 0.0001) and feed efficiency (R 0.992, P < 0.0001). The dephosphorylating ability of phytase in vitro was significantly enhanced (P < 0.05) by the addition of acid phosphatase. Fungal acid protease and Aspergillus niger cellulase also enhanced the dephosphorylation process in vitro.
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PMID:An in vitro procedure for studying enzymic dephosphorylation of phytate in maize-soyabean feeds for turkey poults. 754 27

Mutations located in a new gene, hexY, in Erwinia carotovora ssp. carotovora (Ecc) and ssp. atroseptica (Eca) cause strong upregulation of production of exoenzyme virulence factors and motility. The hexY gene encodes a novel 14.4 kDa protein with no known homologues. The hexY mRNA transcript has an unusually long (525bp) 5' untranslated region, which may be important for post-transcriptional regulation. An elevated level of transcription of two exoenzyme genes, pelCand celV, was observed in the HexY mutant background. The levels of cellulase and protease in a HexY mutant were independent of the presence of PGA, suggesting a role for HexY in the induction of these enzymes seen upon PGA addition. Electron microscopy revealed that HexY cells were hyperflagellated, perhaps contributing to the hypermotility phenotype of this mutant. The HexY mutant M5 exhibited enhanced maceration capacity on potato tubers. Therefore, the hexY gene and its gene product may define another level of regulation of virulence determinants in Ecc and Eca.
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PMID:The hexY genes of Erwinia carotovora ssp. carotovora and ssp. atroseptica encode novel proteins that regulate virulence and motility co-ordinately. 1120 75

Potential feed enzyme additives for ruminants were tested in vitro for their stability to ruminal microbial and gastrointestinal proteolysis. Four commercial preparations from Trichoderma longibrachiatum (A, B, C, and D) and one from an undisclosed source (E) were incubated up to 6 h with ruminal fluid taken from four lactating dairy cows before or 2 h after feeding. The stability of preparation B was also tested in the presence of pepsin at pH 3 and pancreatin at pH 7. Cellulase (EC 3.2.1.4), cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91), beta-glucanase (EC 3.2.1.6), xylanase (EC 3.2.1.8), beta-glucosidase (EC 3.2.1.21), and beta-xylosidase (EC 3.2.1.37) activities were monitored throughout the incubations. Polysaccharidase activities of all enzyme preparations were remarkably stable in ruminal fluid taken after feeding. Ruminal fluid obtained before feeding inactivated the polysaccharidases in preparations B and D to a greater extent than ruminal fluid obtained after feeding. Cellulase and cellulose 1,4-beta-cellobiosidase activities were the least stable, declining (P < 0.05) by 35 and 60% for preparations B and D, respectively. Xylanase activity of preparation D decreased (P < 0.05) by up to 30% after 6 h of incubation, whereas beta-glucanase activity was not affected. The ability to degrade exogenous enzymes also differed among cows (P < 0.05). Pepsin and acid (pH 3.0) did not affect polysaccharidases in preparation B but decreased glycosidase activities by 10 to 15% (P < 0.05) after 1 h of incubation. Pancreatin, at the maximum concentration used, inactivated cellulase, cellulose 1,4-beta-cellobiosidase, and xylanase activities at a rate of 0.55, 1, and 0.45%/min, respectively. beta-Glucosidase and beta-xylosidase activities decreased by 1 and 0.75%/min, respectively. Partial proteolysis of cellulase, cellulose 1,4-beta-cellobiosidase, and xylanase by pancreatin produced a transient increase in activity. This twofold increase for cellulase and fourfold increase for cellulose 1,4-beta-cellobiosidase was directly proportional to pancreatin concentration. These results suggest that the enzyme feed additives tested were stable in the rumen of animals after feeding. Exogenous enzymes are likely to be more susceptible to the host gastrointestinal proteases in the abomasum and intestines than to ruminal proteases. However, exogenous polysaccharidases may survive for a considerable period of time in the small intestine and they probably maintain activity against target substrates in this environment.
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PMID:Resistance of feed enzymes to proteolytic inactivation by rumen microorganisms and gastrointestinal proteases. 1142 1

Highly water-soluble, artificial glycopolypeptides with a gamma-polyglutamic acid (gamma-PGA) backbone derived from Bacillus subtilis sp. and multivalent sialyloligosaccharide units have been chemoenzymatically synthesized as potential polymeric inhibitors of infection by bird and human influenza viruses. 5-Trifluoroacetamidopentyl beta-N-acetyllactosaminide and 5-trifluoroacetamidopentyl beta-lactoside were enzymatically synthesized from LacNAc and lactose, respectively, by cellulase-mediated condensation with 5-trifluoroacetamido-1-pentanol. After deacetylation, the resulting 5-aminopentyl beta-LacNAc and beta-lactoside glycosides were coupled to the alpha-carboxyl groups of the gamma-PGA side chains. The artificial glycopolypeptides carrying LacNAc and lactose were further converted to Neu5Acalpha2-(3/6)Galbeta1-4Glcbeta and Neu5Acalpha2-(3/6)Galbeta1-4GlcNAcbeta sialyloligosaccharide units by alpha2,3- and alpha2,6-sialyltransferase, respectively. The interaction of these glycopolypeptides with various influenza virus strains has been investigated by three different methods. Glycopolypeptides carrying Neu5Acalpha2,6LacNAc inhibited hemagglutination mediated by influenza A and B viruses, and their relative binding affinities for hemagglutinin were 10(2)- to 10(4)-fold higher than that of the naturally occurring fetuin control. A glycopolypeptide carrying Neu5Acalpha2,6LacNAc inhibited infection by A/Memphis/1/71 (H3N2) 93 times more strongly than fetuin, as assessed by cytopathic effects on virus-infected MDCK cells. The avian virus [A/duck/Hong kong/4/78 (H5N3)] bound strongly to Neu5Acalpha2,3LacNAc/Lac-carrying glycopolypeptides, whereas the human virus [A/Memphis/1/71 (H3N2)] bound to Neu5Acalpha2,6LacNAc in preference to Neu5Acalpha2,6Lac. Taken together, these results indicate that the binding of viruses to terminal sialic acids is markedly affected by the structure of the asialo portion, in this case either LacNAc or lactose, in the sugar chain of glycopolypeptides.
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PMID:Chemoenzymatic synthesis of artificial glycopolypeptides containing multivalent sialyloligosaccharides with a gamma-polyglutamic acid backbone and their effect on inhibition of infection by influenza viruses. 1712 32