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Aldo-keto reductase family 1, member D1

AKR1D1, SRD5B1, delta(4)-3-oxosteroid 5beta-reductase
The enzyme encoded by this gene is responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones carrying a delta(4)-3-one structure. Deficiency of this enzyme may contribute to hepatic dysfunction. Three transcript variants encoding different isoforms have been found for this gene. Other variants may be present, but their full-length natures have not been determined yet. [provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: ACID, CAN, STEP, C-9, delta4
Papers on AKR1D1
Shared genetic susceptibility of vascular-related biomarkers with ischemic and recurrent stroke.
New
METASTROKE The Genomics and Randomized Trials Network GARNET Collaborative Research Group et al., Winston-Salem, United States. In Neurology, Jan 2016
We discovered a novel association for CRP level in the AKR1D1 locus (rs2589998, p = 7.3 × 10(-8), approaching genome-wide significance) that also is an expression quantitative trait locus for CRP gene expression.
Single-molecule enzymology of steroid transforming enzymes: Transient kinetic studies and what they tell us.
Review
New
Penning, Philadelphia, United States. In J Steroid Biochem Mol Biol, Nov 2015
We use examples from the hydroxysteroid dehydrogenases (AKR1Cs) and human steroid 5β-reductase (AKR1D1) to illustrate the utility of the approach, which are members of the aldo-keto reductase (AKR) superfamily.
In-Depth Dissection of the P133R Mutation in Steroid 5β-Reductase (AKR1D1): A Molecular Basis of Bile Acid Deficiency.
New
Penning et al., Philadelphia, United States. In Biochemistry, Nov 2015
Human steroid-5β-reductase (aldo-keto reductase 1D1, AKR1D1) stereospecifically reduces Δ(4)-3-ketosteroids to 5β-dihydrosteroids and is essential for steroid hormone metabolism and bile acid biosynthesis.
The rate-determining steps of aldo-keto reductases (AKRs), a study on human steroid 5β-reductase (AKR1D1).
New
Penning et al., Philadelphia, United States. In Chem Biol Interact, Jul 2015
Using human steroid 5β-reductase (AKR1D1) as a representative enzyme, the influence of substrate structure on the rate-limiting steps of AKR catalysis has been previously determined.
The aldo-keto reductases (AKRs): Overview.
Review
New
Penning, Philadelphia, United States. In Chem Biol Interact, Jul 2015
There are 15 human AKRs of these AKR1B1, AKR1C1-1C3, AKR1D1, and AKR1B10 have been implicated in diabetic complications, steroid hormone dependent malignancies, bile acid deficiency and defects in retinoic acid signaling, respectively.
Distinguishing primary from secondary Δ(4) -3-oxosteroid 5β-reductase (SRD5B1, AKR1D1) deficiency by urinary steroid analysis.
New
Kimura et al., Kurume, Japan. In Clin Endocrinol (oxf), Mar 2015
Deficiency of 5β-reductase includes 2 types: primary deficiency, with an SRD5B1 gene mutation; and secondary deficiency, lacking a mutation.
Rate of steroid double-bond reduction catalysed by the human steroid 5β-reductase (AKR1D1) is sensitive to steroid structure: implications for steroid metabolism and bile acid synthesis.
Penning et al., Philadelphia, United States. In Biochem J, 2014
Human AKR1D1 (steroid 5β-reductase/aldo-keto reductase 1D1) catalyses the stereospecific reduction of double bonds in Δ4-3-oxosteroids, a unique reaction that introduces a 90° bend at the A/B ring fusion to yield 5β-dihydrosteroids.
5β-Reduced steroids and human Δ(4)-3-ketosteroid 5β-reductase (AKR1D1).
Review
Penning et al., Philadelphia, United States. In Steroids, 2014
In humans there is only a single 5β-reductase gene AKR1D1, which encodes Δ(4)-3-ketosteroid-5β-reductase (AKR1D1).
Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism.
Review
Penning et al., Ljubljana, Slovenia. In Steroids, 2014
Human aldo-keto reductases AKR1C1-AKR1C4 and AKR1D1 play essential roles in the metabolism of all steroid hormones, the biosynthesis of neurosteroids and bile acids, the metabolism of conjugated steroids, and synthetic therapeutic steroids.
Genetic variation in aldo-keto reductase 1D1 (AKR1D1) affects the expression and activity of multiple cytochrome P450s.
Schuetz et al., Memphis, United States. In Drug Metab Dispos, 2013
Human liver gene regulatory (Bayesian) network analysis was previously used to identify a cytochrome P450 (P450) gene subnetwork with Aldo-keto reductase 1D1 (AKR1D1) as a key regulatory driver of this subnetwork.
Two neonatal cholestasis patients with mutations in the SRD5B1 (AKR1D1) gene: diagnosis and bile acid profiles during chenodeoxycholic acid treatment.
Matsuishi et al., Kurume, Japan. In J Inherit Metab Dis, 2013
BACKGROUND AND AIMS: In two Japanese infants with neonatal cholestasis, 3-oxo-Δ(4)-steroid 5β-reductase deficiency was diagnosed based on mutations of the SRD5B1 gene.
Primary ∆4-3-oxosteroid 5β-reductase deficiency: two cases in China.
Wang et al., Shanghai, China. In World J Gastroenterol, 2013
Aldo-keto reductase 1D1 (AKR1D1) deficiency, a rare but life-threatening form of bile acid deficiency, has not been previously described in China.
A combination of mutations in AKR1D1 and SKIV2L in a family with severe infantile liver disease.
Kelly et al., Birmingham, United Kingdom. In Orphanet J Rare Dis, 2012
A novel homozygous frameshift germline mutation (c.587delG) in the AKR1D1 gene; which encodes the enzyme Δ 4-3-oxosteroid 5β-reductase that is required for synthesis of primary bile acids and is crucial for establishment of normal bile flow, was found in all 3 patients.
Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering.
GeneRIF
Penning et al., Philadelphia, United States. In J Biol Chem, 2012
These studies show how a single point mutation in AKR1D1 can introduce HSD activity with unexpected configurational and stereochemical preference.
The effect of disease associated point mutations on 5β-reductase (AKR1D1) enzyme function.
GeneRIF
Penning et al., Philadelphia, United States. In Chem Biol Interact, 2011
all five mutations identified in patients with functional bile acid deficiency strongly affected AKR1D1 enzyme functionality and therefore may be causal for this disease
Substrate specificity and inhibitor analyses of human steroid 5β-reductase (AKR1D1).
GeneRIF
Penning et al., Philadelphia, United States. In Steroids, 2011
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.
Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency.
GeneRIF
Penning et al., Philadelphia, United States. In J Biol Chem, 2010
analysis of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency
SRD5B1 gene analysis needed for the accurate diagnosis of primary 3-oxo-Delta4-steroid 5beta-reductase deficiency.
GeneRIF
Matsuishi et al., Kurume, Japan. In J Gastroenterol Hepatol, 2009
SRD5B1 gene analysis needed for the accurate diagnosis of primary 3-oxo-Delta4-steroid 5beta-reductase deficiency.
The roles of aldo-keto reductases in steroid hormone action.
Review
Penning et al., Philadelphia, United States. In Drug News Perspect, 2004
Human AKR members that may regulate the local concentration of steroid hormones include: AKR1C1, AKR1C2, AKR1C3, AKR1C4 and AKR1D1.
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