| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.68088813 |
| Mutation analysis of PHYH cDNA from 22 patients with RD revealed 14 different missense mutations , a 3 bp insertion , and a 1 bp deletion , which were all confirmed at the genome level . 0.68088813^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.75230964 |
| Human PAHX is targetted to peroxisomes , requires the PTS 2 receptor for peroxisomal localization , interacts with the PTS 2 receptor in the yeast two hybrid assay and has intrinsic phytanoyl CoA alpha hydroxylase activity that requires the dioxygenase cofactor iron and cosubstrate 2 oxoglutarate . 0.75230964^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.0 |
| Patients affected with Refsum disease ( RD ) have elevated levels of phytanic acid due to a deficiency of the peroxisomal enzyme phytanoyl CoA hydroxylase ( PhyH ) . ^^^ In most patients with RD , disease causing mutations in the PHYH gene have been identified , but , in a subset , no mutations could be found , indicating that the condition is genetically heterogeneous . ^^^ Linkage analysis of a few patients diagnosed with RD , but without mutations in PHYH , suggested a second locus on chromosome 6q22 24 . ^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.0 |
| Molecular basis of Refsum disease : sequence variations in phytanoyl CoA hydroxylase ( PHYH ) and the PTS 2 receptor ( PEX 7 ) . ^^^ Interestingly , Refsum disease is genetically heterogeneous ; two genes , PHYH ( also named PAHX ) and PEX 7 , have been identified to cause Refsum disease , as reviewed in this work . . ^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.0 |
| Refsum disease ( RD ) is biochemically characterized by the excessive accumulation of phytanic acid in tissues and body fluids due to deficiency of phytanoyl CoA hydroxylase ( PAHX ) . ^^^ In this study , we screened three RD patients and identified a novel deletion ( 88 amino acids ) , and a missense mutation ( Arg275Trp ) in the previously reported PAHX cDNA ( Jansen et al . , 1997 ; Mihalik et al . , 1997 ) . ^^^ Moreover , transfection of skin fibroblasts from two RD patients with wild type PAHX gene restored the activity for alpha oxidation of phytanic acid . ^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.0 |
| Many cases of RD are associated with mutations in phytanoyl CoA 2 hydroxylase ( PAHX ) , an Fe ( 2 ) and 2 oxoglutarate ( 2OG ) dependent oxygenase that catalyzes the initial alpha oxidation step in the degradation of phytenic acid in peroxisomes . ^^^ We describe the 10 ray crystallographic structure of PAHX to 2 . 5 A resolution complexed with Fe ( 2 ) and 2OG and predict the molecular consequences of mutations causing RD . ^^^ Of the 15 PAHX residues observed to be mutated in RD patients , 11 cluster in two distinct groups around the Fe ( 2 ) ( Pro ( 173 ) , His ( 175 ) , Gln ( 176 ) , Asp ( 177 ) , and His ( 220 ) ) and 2OG binding sites ( Trp ( 193 ) , Glu ( 197 ) , Ile ( 199 ) , Gly ( 204 ) , Asn ( 269 ) , and Arg ( 275 ) ) . ^^^ |
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| Interacting proteins: O14832 and O00628 |
Pubmed |
SVM Score :0.0 |
| NA |
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