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

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.7.1.17
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RECOMMENDED NAME
GeneOntology No.
4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
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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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
androstenedione degradation
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androgen and estrogen metabolism
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Steroid degradation
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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best substrate
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-
?
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
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?
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
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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
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weak inhibition
4-(2-aminoethyl)benzenesulfonyl fluoride
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weak inhibition
4-amidinophenylmethanesulfonyl fluoride
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weak inhibition
4-nitrophenyl-4-[bis(1,3-benzodioxol-5-yl)(hydroxy)methyl]piperidine-1-carboxylate
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covalent inhibitor
6-carbamimidoylnaphthalen-2-yl 4-carbamimidamidobenzoate
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weak inhibition
7-amino-4-chloro-3-methoxy-1H-2-benzopyran
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weak inhibition
benzamidine
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weak inhibition
eserine
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an acetylcholinesterase inhibitor
leupeptin
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weak inhibition
Neostigmine
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an acetylcholinesterase inhibitor
Trichlorfon
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an acetylcholinesterase inhibitor, weak inhibition
additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-hydroxy-6-oxo-6-phenyl-2,4-hexadienoic acid
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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
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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
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wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
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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
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wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
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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
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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
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wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
PMSF
Mycobacterium tuberculosis;
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pH 7.5, 21°C, recombinant enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WNH4
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33800
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x * 33800, His6-tagged enzyme, estimated from SDS-PAGE
132000
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calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
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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
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sitting drop vapor diffusion method, using 30% (w/v) PEG 3000, 0.1?M CHES, pH 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni affinity column chromatography
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Ni-NTA column chromatography, gel filtration
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recombinant enzyme from Pseudomonas putida strain KT2442
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Source 15Q anion exchange resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain GJ1158
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expressed in Pseudomonas putida strain KT2442
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expressed in Pseudomonas putida strain KT4224
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recombinant expression in Pseudomonas putida strain KT2442
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S114A
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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
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Show AA Sequence (204 entries)
Please use the Sequence Search for a specific query.
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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)