HSD3B2 is the adrenal and gonadal type-2 3beta-hydroxysteroid dehydrogenase/steroid Delta-isomerase. It sequentially oxidizes the 3beta-hydroxyl group with NAD+ and shifts the Delta5 double bond to Delta4, converting pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, and DHEA to androstenedione. These reactions supply corticosteroid, progestin and androgen biosynthesis. HSD3B2 acts at endoplasmic-reticulum membranes and also associates with the mitochondrial inner membrane on the intermembrane-space side. It is highly expressed in adrenal cortex and gonads; damaging variants cause 3beta-hydroxysteroid dehydrogenase deficiency with impaired adrenal and sex-steroid synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | MODIFY | Summary: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Reason: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008498660 SUPPORTS TRANSFER The inherited broad claim is compatible with target biology. Target-specific biochemical or localization evidence supports the more precise replacement. This review does not dispute the ancestral node placement or infer a propagation failure from donor count; the full PAINT tree was not reanalyzed. Proposed replacements: endoplasmic reticulum membrane mitochondrial inner membrane mitochondrial intermembrane space Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells |
| GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | IBA GO_REF:0000033 | MODIFY | Summary: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Reason: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000041225 SUPPORTS TRANSFER The inherited broad claim is compatible with target biology. Target-specific biochemical or localization evidence supports the more precise replacement. This review does not dispute the ancestral node placement or infer a propagation failure from donor count; the full PAINT tree was not reanalyzed. Proposed replacements: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0006694 steroid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA biological-process annotation to steroid biosynthetic process. This is the correct core process: HSD3B2 catalyzes an obligatory early step in the synthesis of all classes of steroid hormones. Reason: Matches the experimentally supported (IDA/IMP) steroid-biosynthetic role of the enzyme and is at an appropriate level of generality for a common upstream step. Supporting Evidence: PMID:1944309 catalyzes the oxidation and isomerization of delta 5-3 beta-hydroxysteroid precursors into delta 4-ketosteroids, thus leading to the formation of all classes of steroid hormones |
| GO:0008207 C21-steroid hormone metabolic process | IBA GO_REF:0000033 | MODIFY | Summary: HSD3B2 directly generates C21 steroid-hormone precursors through its coupled dehydrogenase/isomerase reaction; refine metabolism to biosynthesis. Reason: HSD3B2 directly generates C21 steroid-hormone precursors through its coupled dehydrogenase/isomerase reaction; refine metabolism to biosynthesis. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008498660 SUPPORTS TRANSFER The inherited broad claim is compatible with target biology. Target-specific biochemical or localization evidence supports the more precise replacement. This review does not dispute the ancestral node placement or infer a propagation failure from donor count; the full PAINT tree was not reanalyzed. Proposed replacements: C21-steroid hormone biosynthetic process Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0003854 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA (RHEA/EC 1.1.1.145) annotation of the specific dehydrogenase activity. This is one of the two core molecular functions and is corroborated by experimental IDA/IMP annotations to the same term. Reason: The curated, experimentally supported pregnenolone oxidation reaction (ECO:0000269|PubMed:25322271) demonstrates NAD+-dependent steroid 3beta-hydroxyl oxidation. It supports this core activity independently of the EC label and duplicate annotations. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt Reaction=pregnenolone + NAD(+) = pregn-5-ene-3,20-dione + NADH + H(+); |
| GO:0004022 alcohol dehydrogenase (NAD+) activity | IEA GO_REF:0000116 | MODIFY | Summary: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Reason: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Proposed replacements: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0004769 steroid Delta-isomerase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA (RHEA/EC 5.3.3.1) annotation of the steroid Delta-isomerase activity, the second catalytic function of this bifunctional enzyme (Delta5-3-ketosteroid to Delta4-3-ketosteroid isomerization). Corroborated by experimental IDA/IMP. Reason: The curated, experimentally supported conversion of pregn-5-ene-3,20-dione to progesterone (ECO:0000269|PubMed:25322271) directly expresses the Delta5-to-Delta4 isomerization. It supports this core activity independently of the EC label and duplicate annotations. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt Reaction=pregn-5-ene-3,20-dione = progesterone; |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: IEA annotation from UniProt subcellular-location mapping to endoplasmic reticulum membrane, the primary experimentally supported site of HSD3B2. Consistent with EXP/TAS and IDA (ER) annotations. Reason: Correct primary localization; the enzyme is a single-pass ER-membrane protein. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0006694 steroid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: IEA (InterPro/UniPathway) annotation to steroid biosynthetic process, duplicating the experimentally supported core biological process. Reason: Correct core process, consistent with IDA/IMP/IBA annotations to the same term. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt Lipid metabolism; steroid biosynthesis |
| GO:0006702 androgen biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: DHEA-to-androstenedione conversion is directly assayed for HSD3B2 and is a core androgen-biosynthetic reaction, in adrenal as well as gonadal contexts. Reason: DHEA-to-androstenedione conversion is directly assayed for HSD3B2 and is a core androgen-biosynthetic reaction, in adrenal as well as gonadal contexts. Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | IEA GO_REF:0000002 | MODIFY | Summary: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Reason: The NAD+-dependent oxidation of steroid 3beta-hydroxyl groups is real; refine the broad alcohol/CH-OH oxidoreductase label to the specific steroid dehydrogenase activity already annotated. Proposed replacements: 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000044 | MODIFY | Summary: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Reason: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Proposed replacements: mitochondrial inner membrane Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The interaction-screen protein-binding term is uninformative about the steroidogenic activity. Removal follows the protein-binding policy and does not deny the reported interaction. Reason: The interaction-screen protein-binding term is uninformative about the steroidogenic activity. Removal follows the protein-binding policy and does not deny the reported interaction. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: HSD3B2 has supported endoplasmic reticulum localization, retained separately from its subcompartment annotations. Reason: Retain the curated HPA ER assignment, independently corroborated by the publication-linked UniProt ER-membrane location (PMID:25322271). An organelle-level imaging assignment need not resolve membrane topology. The unrelated mitochondrial observation and steroid-conversion assay are not used as evidence for ER localization. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: Experimental (immunofluorescence/Western in COS-7 cells) localization to the endoplasmic reticulum membrane; the pathogenic G250V variant retained normal ER localization, confirming the wild-type ER-membrane site. Reason: Experimentally supported primary localization; core cellular component. Supporting Evidence: PMID:25322271 p.G250V mutation has no effect on the expression and intracellular localization of the mutant protein |
| GO:0003854 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity | IMP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: IMP evidence: the G250V HSD3B2 mutant showed markedly reduced activity for the NAD+-dependent conversion of pregnenolone to progesterone and DHEA to androstenedione, demonstrating the wild-type 3beta-hydroxy-Delta5-steroid dehydrogenase activity. Reason: Mutant loss-of-function directly supports this core dehydrogenase activity. Supporting Evidence: PMID:25322271 3betaHSD2 is a bifunctional microsomal NAD+-dependent enzyme crucial for adrenal and gonad steroid biosynthesis, converting Ξ5-steroids to Ξ4-steroids |
| GO:0004769 steroid Delta-isomerase activity | IMP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: IMP evidence for the isomerase half of the bifunctional enzyme; the two-step conversion of Delta5 precursors to Delta4 products (impaired by the G250V variant) requires the Delta5-3-ketosteroid isomerase activity. Reason: Mutant loss-of-function supports this core isomerase activity of the bifunctional enzyme. Supporting Evidence: PMID:25322271 3betaHSD2 is a bifunctional microsomal NAD+-dependent enzyme crucial for adrenal and gonad steroid biosynthesis, converting Ξ5-steroids to Ξ4-steroids |
| GO:0005783 endoplasmic reticulum | IMP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: HSD3B2 has supported endoplasmic reticulum localization, retained separately from its subcompartment annotations. Reason: The source describes immunofluorescence and unchanged intracellular localization of the G250V protein; the publication-linked UniProt CC location and variant feature explicitly specify ER localization. Retain that organelle claim with the ER-membrane annotation separately. The accessible abstract does not independently expose the full ER marker experiment; no new image inspection is claimed. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane PMID:25322271 Western blot and immunofluorescence suggested that p.G250V mutation has no effect on the expression and intracellular localization of the mutant protein. |
| GO:0006694 steroid biosynthetic process | IMP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: IMP evidence: loss-of-function HSD3B2 mutation impairs steroid biosynthesis (pregnenolone-to-progesterone and DHEA-to-androstenedione conversion), directly supporting the steroid biosynthetic process role. Reason: Core biological process supported by mutant phenotype and the human CAH disease mechanism. Supporting Evidence: PMID:25322271 3Ξ²HSD2 deficiency is a rare cause of congenital adrenal hyperplasia caused by recessive loss-of-function HSD3B2 mutations |
| GO:0006702 androgen biosynthetic process | IMP PMID:25322271 A novel missense mutation in the HSD3B2 gene, underlying non... | ACCEPT | Summary: DHEA-to-androstenedione conversion is directly assayed for HSD3B2 and is a core androgen-biosynthetic reaction, in adrenal as well as gonadal contexts. Reason: DHEA-to-androstenedione conversion is directly assayed for HSD3B2 and is a core androgen-biosynthetic reaction, in adrenal as well as gonadal contexts. Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-193052 | ACCEPT | Summary: Reactome TAS: the isomerization of pregn-5-ene-3,20-dione to progesterone is catalyzed by 3-beta-HSD associated with the endoplasmic reticulum membrane. Consistent with the experimentally supported ER-membrane localization. Reason: Reactome-curated ER-membrane localization for a specific HSD3B2-catalyzed reaction. Supporting Evidence: Reactome:R-HSA-193052 This reaction is catalyzed by the isomerase activity of 3 beta-HSD, associated with the endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-193073 | ACCEPT | Summary: Reactome TAS: the two-step oxidation/isomerization of DHEA to androstenedione is catalyzed by 3beta-HSD associated with the endoplasmic reticulum membrane. Reason: Reactome-curated ER-membrane localization for an HSD3B2-catalyzed androgen-pathway reaction. Supporting Evidence: Reactome:R-HSA-193073 two-step reaction catalyzed by 3beta-HSD associated with the endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-193961 | ACCEPT | Summary: Reactome TAS: isomerization of pregn-5-ene-3,20-dione-17-ol to 17-hydroxyprogesterone is catalyzed by 3-beta-HSD associated with the endoplasmic reticulum membrane. Reason: Reactome-curated ER-membrane localization for an HSD3B2-catalyzed reaction. Supporting Evidence: Reactome:R-HSA-193961 This reaction is catalyzed by the isomerase activity of 3 beta-HSD, associated with the endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-196350 | ACCEPT | Summary: Reactome TAS: NAD+-dependent dehydrogenation of pregnenolone to pregn-5-ene-3,20-dione by 3beta-HSD associated with the endoplasmic reticulum membrane. Reason: Reactome-curated ER-membrane localization for the HSD3B2 dehydrogenase reaction. Supporting Evidence: Reactome:R-HSA-196350 catalyzed by the 3 beta-hydroxysteroid activity of 3-beta-hydroxysteroid dehydrogenase/isomerase (HSD3B) enzyme associated with the endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-196372 | ACCEPT | Summary: Reactome TAS: NAD+-dependent dehydrogenation of 17-hydroxypregnenolone to pregn-5-ene-3,20-dione-17-ol by 3beta-HSD associated with the endoplasmic reticulum membrane. Reason: Reactome-curated ER-membrane localization for the HSD3B2 dehydrogenase reaction. Supporting Evidence: Reactome:R-HSA-196372 catalyzed by the 3 beta-hydroxysteroid activity of 3-beta-hydroxysteroid dehydrogenase/isomerase (HSD3B) enzyme associated with the endoplasmic reticulum membrane |
| GO:0005783 endoplasmic reticulum | NAS PMID:1944309 Structure and expression of a new complementary DNA encoding... | ACCEPT | Summary: HSD3B2 has supported endoplasmic reticulum localization, retained separately from its subcompartment annotations. Reason: The original NAS assignment comes from the type-II cloning paper, whose accessible abstract identifies the adrenal/gonadal enzyme but does not describe a localization experiment. Later publication-linked UniProt ER localization (PMID:25322271) independently supports the same target claim. Retain ER without attributing membrane topology to the historical source or using separate mitochondrial evidence as ER support. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:human/HSD3B2/HSD3B2-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0031966 mitochondrial membrane | NAS PMID:1944309 Structure and expression of a new complementary DNA encoding... | MODIFY | Summary: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Reason: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Proposed replacements: mitochondrial inner membrane Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells |
| GO:0016020 membrane | NAS PMID:1944309 Structure and expression of a new complementary DNA encoding... | MODIFY | Summary: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Reason: The broad compartment is compatible with HSD3B2 but membrane-associated ER and mitochondrial localizations are resolved more precisely. Mitochondrial association is supported by full-text fractionation/import experiments, including human adrenal cells; it need not mean membrane integration. Proposed replacements: endoplasmic reticulum membrane mitochondrial inner membrane Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Full-text PMID21930695 demonstrates IMM association and IMS-facing interactions and reports localization in human NCI H295 adrenal cells. This is a functional mitochondrial pool, not unsupported specificity; association does not require integral insertion. Reason: Full-text PMID21930695 demonstrates IMM association and IMS-facing interactions and reports localization in human NCI H295 adrenal cells. This is a functional mitochondrial pool, not unsupported specificity; association does not require integral insertion. Supporting Evidence: PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells PMID:21930695 3Ξ²HSD2 specifically associated with the IMM but was not integrated into the membrane |
| GO:0005758 mitochondrial intermembrane space | ISS GO_REF:0000024 | ACCEPT | Summary: Full-text PMID21930695 demonstrates IMM association and IMS-facing interactions and reports localization in human NCI H295 adrenal cells. This is a functional mitochondrial pool, not unsupported specificity; association does not require integral insertion. Reason: Full-text PMID21930695 demonstrates IMM association and IMS-facing interactions and reports localization in human NCI H295 adrenal cells. This is a functional mitochondrial pool, not unsupported specificity; association does not require integral insertion. Supporting Evidence: PMID:21930695 Similarly, 3Ξ²HSD2 also localized to the IMM in human breast cancer MCF-7 cells and human adrenal NCI H295 cells PMID:21930695 3Ξ²HSD2 specifically associated with the IMM but was not integrated into the membrane |
| GO:0030868 smooth endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: The smooth ER membrane is consistent with the steroidogenic microsomal pool and the curated ortholog localization. Retain this compartment without claiming mitochondrial exclusivity. Reason: The smooth ER membrane is consistent with the steroidogenic microsomal pool and the curated ortholog localization. Retain this compartment without claiming mitochondrial exclusivity. Supporting Evidence: PMID:25322271 enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione file:human/HSD3B2/HSD3B2-uniprot.txt Endoplasmic reticulum membrane |
| GO:0003854 3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity | IDA PMID:1944309 Structure and expression of a new complementary DNA encoding... | ACCEPT | Summary: IDA: direct enzymatic assay of expressed type-II 3beta-HSD with NAD+ and 3H-pregnenolone/DHEA demonstrated 3beta-hydroxysteroid dehydrogenase activity (with measured Km values). Core molecular function. Reason: Direct biochemical demonstration of the NAD+-dependent dehydrogenase activity. Supporting Evidence: PMID:1944309 In vitro incubation with NAD+ and 3H-labeled pregnenolone or dehydroepiandrosterone shows that the type I protein possesses a 3 beta HSD/delta 5-delta 4 isomerase activity higher than type II |
| GO:0004769 steroid Delta-isomerase activity | IDA PMID:1944309 Structure and expression of a new complementary DNA encoding... | ACCEPT | Summary: IDA: the same expressed type-II enzyme catalyzed the oxidation and isomerization of Delta5-3beta-hydroxysteroid precursors into Delta4-ketosteroids, demonstrating the steroid Delta-isomerase activity of the bifunctional enzyme. Reason: Direct biochemical demonstration of the Delta5-Delta4 isomerase activity. Supporting Evidence: PMID:1944309 catalyzes the oxidation and isomerization of delta 5-3 beta-hydroxysteroid precursors into delta 4-ketosteroids |
| GO:0006694 steroid biosynthetic process | IDA PMID:1944309 Structure and expression of a new complementary DNA encoding... | ACCEPT | Summary: IDA: the demonstrated dehydrogenase/isomerase activity leads to the formation of all classes of steroid hormones, directly supporting participation in steroid biosynthesis. Core biological process. Reason: Direct experimental support for the steroid biosynthetic role. Supporting Evidence: PMID:1944309 thus leading to the formation of all classes of steroid hormones |
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