We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments The enzyme is involved in the bacterial degradation of the steroid ring structure, and is involved in degradation of multiple steroids, such as testosterone , cholesterol , and sitosterol.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase,
HsaD , TesD,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase
-
-
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase
-
-
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase
-
-
-
HsaD
-
-
TesD
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
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
-
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
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 + ?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
-
-
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 + ?
-
the apparent specificity for 4,59,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid is 34fold higher than for 2-hydroxy-6-oxo-6-phenylpentadienoate
-
-
?
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 + ?
-
the apparent specificity for 4,59,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid is 34fold higher than for 2-hydroxy-6-oxo-6-phenylpentadienoate
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
-
high specificity
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
-
high specificity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
-
high specificity
-
-
?
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
?
-
high specificity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.008
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
0.23
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
apparent value, in 100 mM of phosphate buffer (pH 7.4) with 20 mM NaCl, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.066
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
0.25
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
in 100 mM of phosphate buffer (pH 7.4) with 20 mM NaCl, temperature not specified in the publication
0.000085
4,5-9,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid
-
mutant enzyme S114A, in 100 mM potassium phosphate, pH 7.5, at 25°C
0.55
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1.129
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
apparent value, in 100 mM of phosphate buffer (pH 7.4) with 20 mM NaCl, temperature not specified in the publication
9
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.63
PMSF
Mycobacterium tuberculosis
-
pH 7.5, 21°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
132000
-
calculated from amino acid sequence
33800
-
x * 33800, His6-tagged enzyme, estimated from SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
-
x * 33800, His6-tagged enzyme, estimated from SDS-PAGE
homotetramer
-
x * 33800, His6-tagged enzyme, estimated from SDS-PAGE
-
tetramer
-
x-ray crystallography
tetramer
-
x-ray crystallography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S114A
-
the mutant has a 6500fold lower kcat for 4,59,10-diseco-3-hydroxy-5,9,17-tri-oxoandrosta-1(10),2-diene-4-oic acid compared to the wild type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ni affinity column chromatography
-
Ni-NTA column chromatography, gel filtration
-
recombinant enzyme from Pseudomonas putida strain KT2442
-
Source 15Q anion exchange resin column chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Horinouchi, M.; Hayashi, T.; Yamamoto, T.; Kudo, T.
A new bacterial steroid degradation gene cluster in Comamonas testosteroni TA441 which consists of aromatic-compound degradation genes for seco-steroids and 3-ketosteroid dehydrogenase genes
Appl. Environ. Microbiol.
69
4421-4430
2003
Comamonas testosteroni, Comamonas testosteroni TA441
brenda
Lack, N.; Lowe, E.; Liu, J.; Eltis, L.; Noble, M.; Sim, E.; Westwood, I.
Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
64
2-7
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Lack, N.; Kawamura, A.; Fullam, E.; Laurieri, N.; Beard, S.; Russell, A.; Evangelopoulos, D.; Westwood, I.; Sim, E.
Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis
Biochem. J.
418
369-378
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Lack, N.; Yam, K.; Lowe, E.; Horsman, G.; Owen, R.; Sim, E.; Eltis, L.
Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism
J. Biol. Chem.
285
434-443
2010
Mycobacterium tuberculosis
brenda
Van Der Geize, R.; Yam, K.; Heuser, T.; Wilbrink, M.; Hara, H.; Anderton, M.; Sim, E.; Dijkhuizen, L.; Davies, J.; Mohn, W.; Eltis, L.
A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into Mycobacterium tuberculosis survival in macrophages
Proc. Natl. Acad. Sci. USA
104
1947-1952
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Ryan, A.; Keany, S.; Eleftheriadou, O.; Ballet, R.; Cheng, H.Y.; Sim, E.
Mechanism-based inhibition of HsaD: a C-C bond hydrolase essential for survival of Mycobacterium tuberculosis in macrophage
FEMS Microbiol. Lett.
350
42-47
2014
Mycobacterium tuberculosis
brenda
Select items on the left to see more content.
html completed