AKR1D1 Antibody

1. infant proved to be a compound heterozygote of the AKR1D1 variants c.579+2delT and c.853C>T(p.Q285X), two novel mutations originated from his mother and father, respectively PMID: 28697823
2. Impaired NADPH binding and hydride transfer is the molecular basis for bile acid deficiency in patients with the P133R mutation in AKR1D1. PMID: 26418565
3. When different steroid substrates were used in single turnover experiments with AKR1D1. PMID: 25500266
4. AKR1D1 generates all 5beta-dihydrosteroids in the C19-C27 steroid series. PMID: 24513054
5. Despite having high kchem values with steroid hormones, the kinetic control of AKR1D1 is consistent with the enzyme catalysing the slowest step in the catabolic sequence of steroid hormone transformation in the liver. PMID: 24894951
6. Studies indicate that mutations in aldo-keto reductase family 1 (AKR1) enzymes AKR1C1 and AKR1C4 are responsible for sexual development dysgenesis and mutations in AKR1D1 are causative in bile-acid deficiency. PMID: 24189185
7. Novel homozygous frameshift mutations in the AKR1D1 gene and in the SKIV2L gene were found in a family with severe infantile liver disease. PMID: 23679950
8. Consistent with AKR1D1's putative role as a driver of the P450 subnetwork, the AKR1D1 3'-UTR SNP was significantly associated with increased hepatic mRNA expression of multiple P450s PMID: 23704699
9. These studies show how a single point mutation in AKR1D1 can introduce HSD activity with unexpected configurational and stereochemical preference. PMID: 22437839
10. all five mutations identified in patients with functional bile acid deficiency strongly affected AKR1D1 enzyme functionality and therefore may be causal for this disease PMID: 21185810
11. determined the substrate specificity of homogeneous human recombinant AKR1D1 using C18, C19, C21, and C27 Delta(4)-ketosteroids and assessed the pH-rate dependence of the enzyme. PMID: 21255593
12. analysis of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency PMID: 20522910
13. In placenta and myometrium, relative expression decreased significantly in association with labour, by about two-fold and 10-fold, respectively. These data are consistent with a possible role for 5betaDHP in the onset of spontaneous human labour. PMID: 16123077
14. analysis of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) crystal structure and implications for substrate binding and catalysis PMID: 18407998
15. The structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions, is reported. PMID: 18848863
16. Structure determination of human AKR1C4 and homology modelling of AKR1D1 followed by docking experiments were used to explore active site geometries. PMID: 19013211
17. Delta4-3-ketosteroid 5beta-reductase (AKR1D1) has an alternative binding site responsible for substrate inhibition PMID: 19075558
18. SRD5B1 gene analysis needed for the accurate diagnosis of primary 3-oxo-Delta4-steroid 5beta-reductase deficiency. PMID: 19175828

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HGNC: 388

OMIM: 235555

KEGG: hsa:6718

STRING: 9606.ENSP00000242375

UniGene: Hs.201667