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http://purl.uniprot.org/citations/9211872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9211872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9211872http://www.w3.org/2000/01/rdf-schema#comment"Prolyl 4-hydroxylase (proline hydroxylase, EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens. The vertebrate enzyme is an alpha2beta2 tetramer, the beta subunit of which is identical to protein disulfide-isomerase (PDI, EC 5.3.4.1). We report here on cloning of the recently discovered alpha(II) subunit from human sources. The mRNA for the alpha(II) subunit was found to be expressed in a variety of human tissues, and the presence of the corresponding polypeptide and the (alpha(II))2beta2 tetramer was demonstrated in cultured human WI-38 and HT-1080 cells. The type II tetramer was found to represent about 30% of the total prolyl 4-hydroxylase in these cells and about 5-15% in various chick embryo tissues. The results of coexpression in insect cells argued strongly against the formation of a mixed alpha(I)alpha(II)beta2 tetramer. PDI/beta polypeptide containing a histidine tag in its N terminus was found to form prolyl 4-hydroxylase tetramers as readily as the wild-type PDI/beta polypeptide, and histidine-tagged forms of prolyl 4-hydroxylase appear to offer an excellent source for a simple large scale purification of the recombinant enzyme. The properties of the purified human type II enzyme were very similar to those of the type I enzyme, but the Ki of the former for poly(L-proline) was about 200-1000 times that of the latter. In agreement with this, a minor difference, about 3-6-fold, was found between the two enzymes in the Km values for three peptide substrates. The existence of two forms of prolyl 4-hydroxylase in human cells raises the possibility that mutations in one enzyme form may not be lethal despite the central role of this enzyme in the synthesis of all collagens."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.28.17342"xsd:string
http://purl.uniprot.org/citations/9211872http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.28.17342"xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Myllyharju J."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Myllyharju J."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Kivirikko K.I."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Kivirikko K.I."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Pihlajaniemi T."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Pihlajaniemi T."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Annunen P."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Annunen P."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Helaakoski T."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Helaakoski T."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Veijola J."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/author"Veijola J."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/pages"17342-17348"xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/pages"17342-17348"xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/title"Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer."xsd:string
http://purl.uniprot.org/citations/9211872http://purl.uniprot.org/core/title"Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer."xsd:string
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