| http://purl.uniprot.org/citations/22220568 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22220568 | http://www.w3.org/2000/01/rdf-schema#comment | "Alkylglycerol mono-oxygenase (EC 1.14.16.5) forms a third, distinct, class among tetrahydrobiopterin-dependent enzymes in addition to aromatic amino acid hydroxylases and nitric oxide synthases. Its protein sequence contains the fatty acid hydroxylase motif, a signature indicative of a di-iron centre, which contains eight conserved histidine residues. Membrane enzymes containing this motif, including alkylglycerol mono-oxygenase, are especially labile and so far have not been purified to homogeneity in active form. To obtain a first insight into structure-function relationships of this enzyme, we performed site-directed mutagenesis of 26 selected amino acid residues and expressed wild-type and mutant proteins containing a C-terminal Myc tag together with fatty aldehyde dehydrogenase in Chinese-hamster ovary cells. Among all of the acidic residues within the eight-histidine motif, only mutation of Glu137 to alanine led to an 18-fold increase in the Michaelis-Menten constant for tetrahydrobiopterin, suggesting a role in tetrahydrobiopterin interaction. A ninth additional histidine residue essential for activity was also identified. Nine membrane domains were predicted by four programs: ESKW, TMHMM, MEMSAT and Phobius. Prediction of a part of the structure using the Rosetta membrane ab initio method led to a plausible suggestion for a structure of the catalytic site of alkylglycerol mono-oxygenase."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20111509"xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Golderer G."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Keller M.A."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Werner E.R."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Yarov-Yarovoy V."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Hermetter A."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Hulo N."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Watschinger K."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Werner-Felmayer G."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/author | "Fuchs J.E."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/pages | "279-286"xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/title | "Catalytic residues and a predicted structure of tetrahydrobiopterin-dependent alkylglycerol mono-oxygenase."xsd:string |
| http://purl.uniprot.org/citations/22220568 | http://purl.uniprot.org/core/volume | "443"xsd:string |
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