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Information on EC 1.1.1.51 - 3(or 17)beta-hydroxysteroid dehydrogenase and Organism(s) Comamonas testosteroni and UniProt Accession P19871
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1.1.1.51 3(or 17)beta-hydroxysteroid dehydrogenaseIUBMB Comments
Also acts on other 3beta- or 17beta-hydroxysteroids. cf. EC 1.1.1.209 3(or 17)alpha-hydroxysteroid dehydrogenase.
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Word Map
- 1.1.1.51
- testosterone
- androgen
-
steroidogenic
- progesterone
- estradiol
- adrenal
-
steroidogenesis
- androstenedione
- estrone
- testicular
- aromatase
- testis
- ovarian
- leydig
- 17beta-hsds
- dehydroepiandrosterone
- pregnenolone
- gonad
- lh
-
granulosa
- gonadotropin
-
alpha-reductase
- dihydrotestosterone
- cyp11a1
-
alpha-hydroxylase
- acth
- p450scc
- dheas
- luteal
- progestin
-
sulfatase
- pseudohermaphroditism
- trilostane
- hsd3b1
- genitalia
- p450arom
-
alpha-dihydrotestosterone
-
beta-diol
- hirsutism
-
alpha-hydroxysteroid
- 17-hydroxyprogesterone
-
lhcgr
-
alpha-hydroxyprogesterone
-
virilization
-
17-ketosteroids
- synthesis
- drug development
-
hcg-stimulated
-
pubarche
- srd5a2
- diagnostics
-
17-hydroxylase
- medicine
- environmental protection
-
adrenarche
The taxonomic range for the selected organisms is: Comamonas testosteroni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3 beta-hydroxysteroid dehydrogenase, 17 beta-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase, hsd17b1, hsd17b3, 3betahsd, 17beta-hsd1, 17beta-hydroxysteroid dehydrogenases, 17beta-hydroxysteroid dehydrogenase type 1, 17beta-hsd3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
17-ketoreductase
-
-
-
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17beta-hydroxy steroid dehydrogenase
-
-
-
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3beta,17beta-hydroxysteroid dehydrogenase
-
-
-
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3beta-hydroxy steroid dehydrogenase
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-
-
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3beta-hydroxysteroid dehydrogenase
-
-
-
-
3beta-hydroxystroid oxidoreductase
-
-
-
-
3beta17betaHSDH
-
-
-
-
beta-hydroxy steroid dehydrogenase
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-
-
-
dehydrogenase, 17beta-hydroxy steroid
-
-
-
-
dehydrogenase, 3beta-hydroxy steroid
-
-
-
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dehydrogenase, beta-hydroxy steroid
-
-
-
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steroid 17beta-reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
3(or 17)beta-hydroxysteroid:NAD(P)+ oxidoreductase
Also acts on other 3beta- or 17beta-hydroxysteroids. cf. EC 1.1.1.209 3(or 17)alpha-hydroxysteroid dehydrogenase.
CAS REGISTRY NUMBER
COMMENTARY
9015-81-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
androst-4-ene-3,17-dione + NADPH + H+
testosterone + NADP+
-
-
-
?
testosterone + NAD(P)+
androst-4-en-3,17-dione + NAD(P)H + H+
-
-
-
?
additional information
?
-
the wild-type strain ATCC 119960 degrades steroids, such as testosterone, estradiol, or cholesterol, differences in the enzyme mutant strains, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
androst-4-ene-3,17-dione + NADPH + H+
testosterone + NADP+
-
-
-
?
additional information
?
-
the wild-type strain ATCC 119960 degrades steroids, such as testosterone, estradiol, or cholesterol, differences in the enzyme mutant strains, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.685
3-acetylpyridine adenine dinucleotide
-
testosterone as substrate
0.063
3-pyridinealdehyde adenine dinucleotide
-
testosterone as substrate
0.083
Thionicotinamide adenine dinucleotide
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testosterone as substrate
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
3,17beta-hydroxysteroid dehydrogenase is a member of the short-chain dehydrogenase/reductase (SDR) superfamily
malfunction
compared to the wild-type Comamonas testosteroni, degradation ability of testosterone and cholesterol is almost lost, and degradation of estradiol is decreased in the 3,17beta-HSD knockout mutant. Degradation of testosterone and cholesterol is obviously increased in the 3,17beta-HSD overexpression mutant. The growths in the medium with testosterone, cholesterol or estradiol are impaired in 3,17beta-HSD knockout mutant
metabolism
Comamonas testosteroni strain ATCC11996 is a gram-negative bacterium which can use steroids as carbon and energy source. 3,17beta-HSD is an enzyme which is involved in the complete oxidative degradation of the steroid skeleton, induced in the presence of these compounds in the culture medium
physiological function
3,17beta-hydroxysteroid dehydrogenase is a key enzyme in steroid degradation
additional information
PhaR is a repressor that controls 3,17beta-HSD expression, phaR knock-out mutants grow at higher rates and produce more protein in the presence of steroids as carbon source. PhaR also regulates other genes that relate to steroid degradation. Estradiol and cholesterol both cannot induce betahsd gene expression in both wild-type and mutant Comamonas testosteroni
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
the enzyme has nearly identical subunits that form a tetramer with 222 symmetry. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices
tetramer
-
A3B, 4 * 23500-26700, SDS-PAGE, nonidentical subunits, similar in size, different in charge
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion technique, crystallographic analysis at 1.2 A resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a betahsd knockout mutant of Comamonas testosteroni by homologous integration, and preparation of 3,17b-HSD gene high expression mutant
additional information
construction of transcriptional repressor PhaR knockout mutants M6 of Comamonas testosteroni, the mutants grow better than wild-type Comamonas testosteroni in the presence of 1 mM testosterone, 0.5 mM estradiol or 0.5 mM cholesterol. phaR Knockout mutants M6 cells are inhibited by estradiol and cholesterol, this inhibition is stronger in M6 cells than in wild-type Comamonas testosteroni
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 mM potassium phosphate buffer, pH 7.5, 1 mM dithiothreitol, 50% glycerol, at least 7 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene betahsd, cloning of PhaR and 3,17beta-HSD together with their promoter domains into plasmids pK18 and pUC19 and coexpression in Escherichia coli strain HB101. A 2509 bp DNA fragment, that contains a putative promoter for the bhsd gene (without the phaR gene), is cloned into plasmid pUC2.5-3. The plasmid is transformed into strain HB101 and induced with testosterone. 3,17beta-HSD expression results at a high level, but cannot be further enhanced by testosterone. Recombinant expression of His-tagged enzyme in Escherichia coli strain BL21. Promoter cloning
gene betahsd, sequence comparisons, cloning and location of the TSS and promoter (126 bp) of the 3,17beta-HSD gene, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3,17beta-HSD gene expression is induced by testosterone, but not by estradiol and cholesterol
estradiol and cholesterol both cannot induce betahsd gene expression in both wild-type and mutant Comamonas testosteroni
the transcriptional repressor phaR gene (phaR) locates 2290 bp upstream of the betahsd gene and might bind on a special bhsd promoter domain
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
transcriptional repressor phaR knockout mutants have better ability to degrade steroids than wild-type Comamonas testosteroni ATCC11996 and might therefore be used in bioremediation
synthesis
engineering Mycobacterium smegmatis for testosterone production. Mycobacterium smegmatis is an excellent chassis to develop biotechnological processes for the biotransformation of sterols and their derivatives into valuable pharmaceutical compounds. Overexpression of the gene encoding microbial 17beta-hydroxysteroid: NADP 17-oxidoreductase, from the bacterium Comamonas testosteroni. The host strains are Mycobacterium smegmatis wild type and a genetic engineered androst-4-ene-3,17-dione producing mutant. The recombinant strains are able to produce testosterone from androst-4-ene-3,17-dione and/or from sterols with high yields
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schultz, R.M.; Groman, E.V.; Engel, L.L.
3(17)beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. Ligand binding properties
J. Biol. Chem.
252
3784-3790
1977
Comamonas testosteroni
Schultz, R.M.; Groman, E.V.; Engel, L.L.
3(17)beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. A convenient purification and demonstration of multiple molecular forms
J. Biol. Chem.
252
3775-3783
1977
Comamonas testosteroni
Minard, P.; Legoy, M.D.; Thomas, D.
3beta, 17beta-Hydroxysteroid dehydrogenase of Pseudomonas testosteroni. Kinetic evidence for the bifunctional activity at a common catalytic site
FEBS Lett.
188
85-90
1985
Comamonas testosteroni
Benach, J.; Knapp, S.; Oppermann, UC.; Hagglund, O.; Jornvall, H.; Ladenstein, R.
Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996
Eur. J. Biochem.
236
144-148
1996
Comamonas testosteroni, Comamonas testosteroni ATTC 11996
Benach, J.; Filling, C.; Oppermann, U.C.; Roversi, P.; Bricogne, G.; Berndt, K.D.; Jornvall, H.; Ladenstein, R.
Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition
Biochemistry
41
14659-14668
2002
Comamonas testosteroni (P19871), Comamonas testosteroni
Yu, Y.; Liu, C.; Wang, B.; Li, Y.; Zhang, H.
Characterization of 3,17beta-hydroxysteroid dehydrogenase in Comamonas testosteroni
Chem. Biol. Interact.
234
221-228
2015
Comamonas testosteroni (P19871), Comamonas testosteroni ATCC 119960 (P19871)
Li, M.; Xiong, G.; Maser, E.
A novel transcriptional repressor PhaR for the steroid-inducible expression of the 3,17beta-hydroxysteroid dehydrogenase gene in Comamonas testosteroni ATCC11996
Chem.-Biol. Interact.
202
116-125
2013
Comamonas testosteroni (P19871), Comamonas testosteroni ATCC 119960 (P19871)
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