| http://purl.uniprot.org/citations/16759730 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16759730 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16759730 | http://www.w3.org/2000/01/rdf-schema#comment | "Contemporary phytase research is primarily concerned with ameliorating the problem of inadequate digestion of inositol hexakisphosphate (phytate; InsP6) in monogastric farm animal feed, so as to reduce the pollution that results from the high phosphate content of the manure. In the current study we pursue a new, safe and cost-effective solution. We demonstrate that the rate of hydrolysis of InsP6 by recombinant avian MINPP (0.7 micromol/mg protein/min) defines it as by far the most active phytase found to date in any animal cell (the corresponding activity of recombinant mammalian MINPP is only 0.006 micromol/mg protein/min). Although avian MINPP has less than 20% sequence identity with microbial phytases, we create a homology model of MINPP in which it is predicted that the structure of the phytase active site is well-conserved. This model is validated by site-directed mutagenesis and by use of a substrate analogue, scyllo-InsP6, which we demonstrate is only a weak MINPP substrate. In a model chicken cell line, we overexpressed a mutant form of MINPP that is secretion-competent. This version of the enzyme was actively secreted without affecting either cell viability or the cellular levels of any inositol phosphates. Our studies offer a genetic strategy for greatly improving dietary InsP6 digestion in poultry."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jbiotec.2006.04.028"xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jbiotec.2006.04.028"xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Cho J."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Cho J."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Shears S.B."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Shears S.B."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Choi K."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Choi K."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Reynolds P.R."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Reynolds P.R."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Petitte J.N."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Petitte J.N."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Darden T."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/author | "Darden T."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/name | "J. Biotechnol."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/name | "J. Biotechnol."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/pages | "248-259"xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/pages | "248-259"xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/title | "Avian multiple inositol polyphosphate phosphatase is an active phytase that can be engineered to help ameliorate the planet's 'phosphate crisis'."xsd:string |
| http://purl.uniprot.org/citations/16759730 | http://purl.uniprot.org/core/title | "Avian multiple inositol polyphosphate phosphatase is an active phytase that can be engineered to help ameliorate the planet's 'phosphate crisis'."xsd:string |