AKR1C1: Difference between revisions

AKR1C1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1MRQ, 3C3U, 3GUG, 3NTY, 4YVP
Identifiers
Aliases	AKR1C1, 2-ALPHA-HSD, 20-ALPHA-HSD, C9, DD1, DD1/DD2, DDH, DDH1, H-37, HAKRC, HBAB, MBAB, aldo-keto reductase family 1, member C1, aldo-keto reductase family 1 member C1
External IDs	OMIM: 600449; MGI: 1924587; HomoloGene: 134114; GeneCards: AKR1C1; OMA:AKR1C1 - orthologs
EC number	1.1.1.112
Gene location (Human)
Chr.	Chromosome 10 (human)
End	4,983,283 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	4,636,540 bp
RNA expression pattern
	Top expressed in
	islet of Langerhans; ; gastric mucosa; ; right lobe of liver; ; right auricle; ; olfactory zone of nasal mucosa; ; body of stomach; ; left coronary artery; ; ascending aorta; ; Descending thoracic aorta; ; gallbladder;
	Top expressed in
	right kidney; ; human kidney; ; proximal tubule; ; morula; ; embryo; ; primary oocyte; ; primary visual cortex; ; secondary oocyte; ; blastocyst; ; muscle of thigh;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; alditol:NADP+ 1-oxidoreductase activity; indanol dehydrogenase activity; aldo-keto reductase (NADP) activity; 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity; androsterone dehydrogenase (B-specific) activity; phenanthrene 9,10-monooxygenase activity; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; bile acid binding; protein binding; carboxylic acid binding; oxidoreductase activity; ketosteroid monooxygenase activity; alcohol dehydrogenase (NADP+) activity; steroid dehydrogenase activity;
Cellular component	cytoplasm; cytosol; extracellular exosome;
Biological process	cellular response to jasmonic acid stimulus; epithelial cell differentiation; daunorubicin metabolic process; doxorubicin metabolic process; progesterone metabolic process; bile acid metabolic process; digestion; retinal metabolic process; retinoid metabolic process; response to organophosphorus; bile acid and bile salt transport; intestinal cholesterol absorption; xenobiotic metabolic process; cholesterol homeostasis; protein homooligomerization; steroid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	1645
	77337
	ENSG00000187134
	ENSMUSG00000021207
	Q04828
	Q91WR5
	NM_001353
	NM_029901
	NP_001344
	NP_084177
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 15:16, 12 May 2024

Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.^[5]^[6]

Superfamily of enzymes

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This specific enzyme, AKR1C1, among other reactions, catalyzes the reduction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. The AKR1C1 gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.^[6]

Isozymes of aldo-keto reductase family 1 member C


HGNC Gene Symbol	Enzyme Name Aliases^[7]
AKR1C1	aldo-keto reductase family 1 member C1; 20α-hydroxysteroid dehydrogenase
AKR1C2	aldo-keto reductase family 1 member C2; 3α-hydroxysteroid dehydrogenase type 3
AKR1C3	aldo-keto reductase family 1 member C3; 3α-hydroxysteroid dehydrogenase type 2; 17β-hydroxysteroid dehydrogenase type 5; HSD17B5
AKR1C4	aldo-keto reductase family 1 member C4; 3α-hydroxysteroid dehydrogenase type 1

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000187134 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021207 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ciaccio PJ, Tew KD (Jun 1994). "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1186 (1–2): 129–32. doi:10.1016/0005-2728(94)90144-9. PMID 8011662.
^ ^a ^b "Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)".
^ Dufort I, Labrie F, Luu-The V (February 2001). "Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution". J Clin Endocrinol Metab. 86 (2): 841–6. doi:10.1210/jcem.86.2.7216. PMID 11158055. human types 1 and 3 3α-HSD, 20α-HSD, and type 5 17β-HSD were named AKR1C4, AKR1C2, AKR1C1, and AKR1C3, respectively

External links

Human AKR1C1 genome location and AKR1C1 gene details page in the UCSC Genome Browser.
Human C9 genome location and C9 gene details page in the UCSC Genome Browser.

Ciaccio PJ, Jaiswal AK, Tew KD (Jun 1994). "Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics". The Journal of Biological Chemistry. 269 (22): 15558–62. doi:10.1016/S0021-9258(17)40716-2. PMID 7515059.
Khanna M, Qin KN, Cheng KC (Jun 1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans". The Journal of Steroid Biochemistry and Molecular Biology. 53 (1–6): 41–6. doi:10.1016/0960-0760(95)00019-V. PMID 7626489. S2CID 11316547.
Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC (Jan 1995). "Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization". Genomics. 25 (2): 588–90. doi:10.1016/0888-7543(95)80066-U. PMID 7789999.
Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A (Mar 1994). "Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding". The Journal of Biological Chemistry. 269 (11): 8416–22. doi:10.1016/S0021-9258(17)37210-1. PMID 8132567.
Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A (Apr 1994). "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder". The Biochemical Journal. 299 (2): 545–52. doi:10.1042/bj2990545. PMC 1138306. PMID 8172617.
Qin KN, New MI, Cheng KC (Dec 1993). "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase". The Journal of Steroid Biochemistry and Molecular Biology. 46 (6): 673–9. doi:10.1016/0960-0760(93)90308-J. PMID 8274401. S2CID 36210133.
Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE (May 1993). "cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family". The Journal of Biological Chemistry. 268 (14): 10448–57. doi:10.1016/S0021-9258(18)82220-7. PMID 8486699.
Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N (Jan 1996). "Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells". The Biochemical Journal. 313 (2): 373–6. doi:10.1042/bj3130373. PMC 1216918. PMID 8573067.
O'connor T, Ireland LS, Harrison DJ, Hayes JD (Oct 1999). "Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members". The Biochemical Journal. 343 (2): 487–504. doi:10.1042/bj3430487. PMC 1220579. PMID 10510318.
Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S (Feb 2000). "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes". Genes to Cells. 5 (2): 111–25. doi:10.1046/j.1365-2443.2000.00310.x. PMID 10672042. S2CID 25136637.
Zhang Y, Dufort I, Rheault P, Luu-The V (Oct 2000). "Characterization of a human 20alpha-hydroxysteroid dehydrogenase". Journal of Molecular Endocrinology. 25 (2): 221–8. doi:10.1677/jme.0.0250221. PMID 11013348.
Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX (Nov 2001). "Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution". The Journal of Biological Chemistry. 276 (45): 42091–8. doi:10.1074/jbc.M105610200. PMID 11514561.
Chen CY, Hsu CP, Hsu NY, Shih CS, Lin TY, Chow KC (2002). "Expression of dihydrodiol dehydrogenase in the resected stage I non-small cell lung cancer". Oncology Reports. 9 (3): 515–9. doi:10.3892/or.9.3.515. PMID 11956619.
Yang MD, Wu CC, Chiou SH, Chiu CF, Lin TY, Chiang IP, Chow KC (2003). "Reduction of dihydrodiol dehydrogenase expression in resected hepatocellular carcinoma". Oncology Reports. 10 (2): 271–6. doi:10.3892/or.10.2.271. PMID 12579257.
Nakajima T, Yasuda K, Nishizawa M, Okada H, Yoshimura T, Ito S, Kanzaki H (Feb 2003). "Expression of 20alpha-hydroxysteroid dehydrogenase mRNA in human endometrium and decidua". Endocrine Journal. 50 (1): 105–11. doi:10.1507/endocrj.50.105. PMID 12733716.
Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R (Aug 2003). "Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids". Journal of Molecular Biology. 331 (3): 593–604. doi:10.1016/S0022-2836(03)00762-9. PMID 12899831.
Agapova OA, Yang P, Wang WH, Lane DA, Clark AF, Weinstein BI, Hernandez MR (Oct 2003). "Altered expression of 3 alpha-hydroxysteroid dehydrogenases in human glaucomatous optic nerve head astrocytes". Neurobiology of Disease. 14 (1): 63–73. doi:10.1016/S0969-9961(03)00101-3. PMID 13678667. S2CID 21159141.

This article on a gene on human chromosome 10 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000187134 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021207 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8011662-5] Ciaccio PJ, Tew KD (Jun 1994). "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1186 (1–2): 129–32. doi:10.1016/0005-2728(94)90144-9. PMID 8011662.

[entrez-6] "Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)".

[pmid11158055-7] Dufort I, Labrie F, Luu-The V (February 2001). "Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution". J Clin Endocrinol Metab. 86 (2): 841–6. doi:10.1210/jcem.86.2.7216. PMID 11158055. human types 1 and 3 3α-HSD, 20α-HSD, and type 5 17β-HSD were named AKR1C4, AKR1C2, AKR1C1, and AKR1C3, respectively

[1]

[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 1: / Line 1: @@
+{{Short description|Protein-coding gene in the species Homo sapiens}}
 {{Infobox_gene}}
-'''Aldo-keto reductase family 1 member C1''' also known as '''[[20α-hydroxysteroid dehydrogenase]]''', '''3α-hydroxysteroid dehydrogenase''', and '''dihydrodiol dehydrogenase 1/2''' is an [[enzyme]] that in humans is encoded by the ''AKR1C1'' [[gene]].<ref name="pmid8011662">{{cite journal | vauthors = Ciaccio PJ, Tew KD | title = cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1186 | issue = 1–2 | pages = 129–32 | date = Jun 1994 | pmid = 8011662 | pmc =  | doi = 10.1016/0005-2728(94)90144-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1645| accessdate = }}</ref>
+'''Aldo-keto reductase family 1 member C1''' also known as '''[[20α-hydroxysteroid dehydrogenase]]''', '''[[3α-Hydroxysteroid dehydrogenase|3α-hydroxysteroid dehydrogenase]]''', and '''dihydrodiol dehydrogenase 1/2''' is an [[enzyme]] that in humans is encoded by the ''AKR1C1'' [[gene]].<ref name="pmid8011662">{{cite journal | vauthors = Ciaccio PJ, Tew KD | title = cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase | journal = Biochimica et Biophysica Acta (BBA) - Bioenergetics | volume = 1186 | issue = 1–2 | pages = 129–32 | date = Jun 1994 | pmid = 8011662 | doi = 10.1016/0005-2728(94)90144-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1645}}</ref>
+==Superfamily of enzymes==
-This gene encodes a member of the [[aldo-keto reductase|aldo/keto reductase superfamily]], which consists of more than 40 known [[enzyme]]s and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of [[progesterone]] to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.<ref name="entrez"/>
+This gene encodes a member of the [[aldo-keto reductase|aldo/keto reductase superfamily]], which consists of more than 40 known [[enzyme]]s and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This specific enzyme, AKR1C1, among other reactions, catalyzes the reduction of [[progesterone]] to the inactive form [[20-alpha-hydroxy-progesterone]]. The ''AKR1C1'' gene shares high sequence identity with three other gene members, and is clustered with those three genes at chromosome 10p15-p14.<ref name="entrez"/>
+==Isozymes of aldo-keto reductase family 1 member C==
+{{AKR1CN}}
 == References ==
 {{reflist}}
+== See also ==
+* [[3α-Hydroxysteroid dehydrogenase]]
 ==External links==
@@ Line 13: / Line 22: @@
 == Further reading ==
 {{refbegin | 2}}
-* {{cite journal | vauthors = Ciaccio PJ, Jaiswal AK, Tew KD | title = Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics | journal = The Journal of Biological Chemistry | volume = 269 | issue = 22 | pages = 15558–62 | date = Jun 1994 | pmid = 7515059 | doi =  }}
+* {{cite journal | vauthors = Ciaccio PJ, Jaiswal AK, Tew KD | title = Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics | journal = The Journal of Biological Chemistry | volume = 269 | issue = 22 | pages = 15558–62 | date = Jun 1994 | doi = 10.1016/S0021-9258(17)40716-2 | pmid = 7515059 | doi-access = free }}
-* {{cite journal | vauthors = Khanna M, Qin KN, Cheng KC | title = Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 53 | issue = 1–6 | pages = 41–6 | date = Jun 1995 | pmid = 7626489 | doi = 10.1016/0960-0760(95)00019-V | s2cid = 11316547 }}
+* {{cite journal | vauthors = Khanna M, Qin KN, Cheng KC | title = Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 53 | issue = 1–6 | pages = 41–6 | date = Jun 1995 | pmid = 7626489 | doi = 10.1016/0960-0760(95)00019-V | s2cid = 11316547 | doi-access = free }}
-* {{cite journal | vauthors = Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC | title = Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization | journal = Genomics | volume = 25 | issue = 2 | pages = 588–90 | date = Jan 1995 | pmid = 7789999 | doi = 10.1016/0888-7543(95)80066-U }}
+* {{cite journal | vauthors = Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC | title = Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization | journal = Genomics | volume = 25 | issue = 2 | pages = 588–90 | date = Jan 1995 | pmid = 7789999 | doi = 10.1016/0888-7543(95)80066-U | doi-access = free }}
-* {{cite journal | vauthors = Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A | title = Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding | journal = The Journal of Biological Chemistry | volume = 269 | issue = 11 | pages = 8416–22 | date = Mar 1994 | pmid = 8132567 | doi =  }}
+* {{cite journal | vauthors = Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A | title = Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding | journal = The Journal of Biological Chemistry | volume = 269 | issue = 11 | pages = 8416–22 | date = Mar 1994 | doi = 10.1016/S0021-9258(17)37210-1 | pmid = 8132567 | doi-access = free }}
 * {{cite journal | vauthors = Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A | title = Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder | journal = The Biochemical Journal | volume = 299 | issue = 2 | pages = 545–52 | date = Apr 1994 | pmid = 8172617 | pmc = 1138306 | doi =  10.1042/bj2990545}}
 * {{cite journal | vauthors = Qin KN, New MI, Cheng KC | title = Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 46 | issue = 6 | pages = 673–9 | date = Dec 1993 | pmid = 8274401 | doi = 10.1016/0960-0760(93)90308-J | s2cid = 36210133 }}
-* {{cite journal | vauthors = Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE | title = cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family | journal = The Journal of Biological Chemistry | volume = 268 | issue = 14 | pages = 10448–57 | date = May 1993 | pmid = 8486699 | doi =  }}
+* {{cite journal | vauthors = Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE | title = cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family | journal = The Journal of Biological Chemistry | volume = 268 | issue = 14 | pages = 10448–57 | date = May 1993 | doi = 10.1016/S0021-9258(18)82220-7 | pmid = 8486699 | doi-access = free }}
 * {{cite journal | vauthors = Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N | title = Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells | journal = The Biochemical Journal | volume = 313 | issue = 2 | pages = 373–6 | date = Jan 1996 | pmid = 8573067 | pmc = 1216918 | doi =  10.1042/bj3130373}}
 * {{cite journal | vauthors = O'connor T, Ireland LS, Harrison DJ, Hayes JD | title = Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members | journal = The Biochemical Journal | volume = 343 | issue = 2 | pages = 487–504 | date = Oct 1999 | pmid = 10510318 | pmc = 1220579 | doi = 10.1042/bj3430487 }}
-* {{cite journal | vauthors = Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S | title = Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes | journal = Genes to Cells | volume = 5 | issue = 2 | pages = 111–25 | date = Feb 2000 | pmid = 10672042 | doi = 10.1046/j.1365-2443.2000.00310.x | s2cid = 25136637 }}
+* {{cite journal | vauthors = Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S | title = Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes | journal = Genes to Cells | volume = 5 | issue = 2 | pages = 111–25 | date = Feb 2000 | pmid = 10672042 | doi = 10.1046/j.1365-2443.2000.00310.x | s2cid = 25136637 | doi-access = free }}
 * {{cite journal | vauthors = Zhang Y, Dufort I, Rheault P, Luu-The V | title = Characterization of a human 20alpha-hydroxysteroid dehydrogenase | journal = Journal of Molecular Endocrinology | volume = 25 | issue = 2 | pages = 221–8 | date = Oct 2000 | pmid = 11013348 | doi = 10.1677/jme.0.0250221 | doi-access = free }}
 * {{cite journal | vauthors = Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX | title = Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42091–8 | date = Nov 2001 | pmid = 11514561 | doi = 10.1074/jbc.M105610200 | doi-access = free }}

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase Alcohol oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)