Information on EC 3.7.1.17 - 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase

for references in articles please use BRENDA:EC3.7.1.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
3.7.1.17
-
top print hide
RECOMMENDED NAME
GeneOntology No.
4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(1E,2Z)-3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate + H2O = 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate + (2Z,4Z)-2-hydroxyhexa-2,4-dienoate
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
androstenedione degradation
-
-
androgen and estrogen metabolism
-
-
Steroid degradation
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase ( (2Z,4Z)-2-hydroxyhexa-2,4-dienoate-forming)
The enzyme is involved in the bacterial degradation of the steroid ring structure, and is involved in degradation of multiple steroids, such as testosterone [1], cholesterol [2], and sitosterol.
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
show the reaction diagram
4,5-9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid + H2O
9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid + 2-hydroxy-hexa-2,4-dienoic acid
show the reaction diagram
-
best substrate
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-dien-4-oic acid + H2O
9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid + 2-hydroxyhexa-2,4-dienoic acid
show the reaction diagram
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid + ?
show the reaction diagram
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
show the reaction diagram
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
top print hide
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
show the reaction diagram
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
-
a broad spectrum covalent inhibitor of serine proteases, the structural homologues of 3,4-dichloroisocoumarin, 7-amino-4-chloro-3-methoxy-1H-2-benzopyran and 3-phenyl-1H-2-benzopyran-1-one, show significantly poorer inhibition
3-phenyl-1H-2-benzopyran-1-one
-
weak inhibition
4-(2-aminoethyl)benzenesulfonyl fluoride
-
weak inhibition
4-amidinophenylmethanesulfonyl fluoride
-
weak inhibition
4-nitrophenyl-4-[bis(1,3-benzodioxol-5-yl)(hydroxy)methyl]piperidine-1-carboxylate
-
covalent inhibitor
6-carbamimidoylnaphthalen-2-yl 4-carbamimidamidobenzoate
-
weak inhibition
7-amino-4-chloro-3-methoxy-1H-2-benzopyran
-
weak inhibition
benzamidine
-
weak inhibition
eserine
-
an acetylcholinesterase inhibitor
leupeptin
-
weak inhibition
Neostigmine
-
an acetylcholinesterase inhibitor
Trichlorfon
-
an acetylcholinesterase inhibitor, weak inhibition
additional information
-
inhibition of HsaD by serine protease inhibitors. No inhibition by acetylcholinesterase inhibitors edrophonium, tacrine, and pyridostigmine. Consistent with the lack of a cysteine residue in the active site of HsaD, covalent inhibitor nicotinamide does not significantly inhibit HsaD
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-hydroxy-6-oxo-6-phenyl-2,4-hexadienoic acid
-
in 20 mM HEPES, 80 mM NaCl, at pH 8.0 and 25°C
0.008 - 0.23
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.017
4,5-9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
0.31
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066 - 0.25
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.000085 - 0.55
4,5-9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid
0.33
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
top print hide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.129 - 9
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
33
4,5-9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
1.06
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
top print hide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
PMSF
Mycobacterium tuberculosis
-
pH 7.5, 21°C, recombinant enzyme
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33800
-
x * 33800, His6-tagged enzyme, estimated from SDS-PAGE
132000
-
calculated from amino acid sequence
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
top print hide
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant enzyme S114A, sitting drop vapor diffusion method, using 200 mM KSCN, 24% polyethylene glycol 3.35 K, and 100 mM bis-tris propane, pH 7.0
-
sitting drop vapor diffusion method, using 30% (w/v) PEG 3000, 0.1?M CHES, pH 9.5
-
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
-
the enzyme retains more than 95% of its activity after incubation at 60°C for 30 min. Hydrolytic activity is significantly decreased after incubation at 70°C
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni affinity column chromatography
-
Ni-NTA column chromatography, gel filtration
-
recombinant enzyme from Pseudomonas putida strain KT2442
-
Source 15Q anion exchange resin column chromatography
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain GJ1158
-
expressed in Pseudomonas putida strain KT2442
-
expressed in Pseudomonas putida strain KT4224
-
recombinant expression in Pseudomonas putida strain KT2442
-
top print hide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S114A
-
the mutant has a 6500fold lower kcat for 4,5–9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid compared to the wild type enzyme
top
Show AA Sequence (204 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 3.7.1.17)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)