| http://purl.uniprot.org/citations/16885164 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16885164 | http://www.w3.org/2000/01/rdf-schema#comment | "Three hypoxia-inducible factor prolyl 4-hydroxylases (HIF-P4Hs) regulate the HIFs by hydroxylating prolines at two separate sites in the oxygen-dependent degradation domain (ODDD) of their alpha subunits. We compared in vitro hydroxylation by purified recombinant human HIF-P4Hs of 19-20- and 35-residue peptides corresponding to the two sites in HIF-alphas and purified recombinant HIF-1alpha and HIF-2alpha ODDDs of 248 and 215 residues. The increase in the length of peptides representing the C-terminal site from 19 to 20 to 35 residues reduced the K(m) values to 90-800 nm, i.e. to 0.7-11% of those for the shorter peptides, whereas those representing the N-terminal site were 10-470 microm, i.e. 10-135%. The K(m) values of HIF-P4H-1 for the recombinant HIF-alpha ODDDs were 10-20 nm, whereas those of HIF-P4H-2 and -3 were 60-140 nm, identical values being found for the wild-type HIF-1alpha ODDD and its N site mutant. The K(m) values for the C site mutant were about 5-10 times higher but only 0.2-3% of those for the 35-residue N site peptides, and this marked difference suggested that the HIF-P4Hs may become bound first to the C-terminal site of an ODDD and that this binding may enhance subsequent binding to the N-terminal site. The K(m) values of HIF-P4H-2 for oxygen determined with the HIF-1alpha ODDD and both its mutants as substrates were all about 100 microm, being 40% of those reported for the three HIF-P4Hs with a 19-residue peptide. Even this value is high compared with tissue O(2) levels, indicating that HIF-P4Hs are effective oxygen sensors."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m604628200"xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/author | "Myllyharju J."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/author | "Koivunen P."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/author | "Kivirikko K.I."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/author | "Hirsila M."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/pages | "28712-28720"xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/title | "The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases."xsd:string |
| http://purl.uniprot.org/citations/16885164 | http://purl.uniprot.org/core/volume | "281"xsd:string |
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