Information on EC 3.1.2.B5 - 3,4-hydroxyphenylacetyl-CoA thioesterase

for references in articles please use BRENDA:EC3.1.2.B5
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.2.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
3,4-hydroxyphenylacetyl-CoA thioesterase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3,4-dihydroxyphenylacetyl-CoA + H2O = 3,4-dihydroxyphenylacetate + CoA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
3,4-dihydroxyphenylacetyl-CoA hydrolase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylacetyl-CoA + H2O
3,4-dihydroxyphenylacetate + CoA
show the reaction diagram
3,5-dihydroxyphenylacetyl-CoA + H2O
3,5-dihydroxyphenylacetate + CoA
show the reaction diagram
3-hydroxyphenylacetyl-CoA + H2O
3-hydroxyphenylacetate + CoA
show the reaction diagram
4-hydroxyphenylacetyl-CoA + H2O
4-hydroxyphenylacetate + CoA
show the reaction diagram
phenylacetyl-CoA + H2O
phenylacetate + CoA
show the reaction diagram
additional information
?
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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
3,4-dihydroxyphenylacetyl-CoA + H2O
3,4-dihydroxyphenylacetate + CoA
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxyphenylacyl-CoA
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4-hydroxyphenylacyl-CoA
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0086 - 0.13
3,4-dihydroxyphenylacetyl-CoA
0.028 - 0.2
3,5-dihydroxyphenylacetyl-CoA
0.021 - 0.23
3-hydroxyphenylacetyl-CoA
0.018 - 0.28
4-hydroxyphenylacetyl-CoA
0.0096 - 0.39
phenylacetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065 - 100
3,4-dihydroxyphenylacetyl-CoA
2.3 - 9
3,5-dihydroxyphenylacetyl-CoA
0.065 - 86
3-hydroxyphenylacetyl-CoA
0.17 - 79
4-hydroxyphenylacetyl-CoA
0.41 - 3.7
phenylacetyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 6250
3,4-dihydroxyphenylacetyl-CoA
45 - 80
3,5-dihydroxyphenylacetyl-CoA
0.7 - 4095
3-hydroxyphenylacetyl-CoA
0.7 - 2257
4-hydroxyphenylacetyl-CoA
10 - 43
phenylacetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 0.039
4-hydroxyphenylacyl-CoA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16419
4 * 16419, ESI mass spectrometry
58000
gel filtration
67000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal His-tagged enzyme is prepared for crystallization. The N-terminal Met is replaced by Ser-Leu. Crystals of the selenomethionine enzyme are grown in 13% polyethylene glycol, 0.1 M [bis(2-hydroxyethyl)imino]-tris(hydroxymethyl)methane (pH 6.0) and 0.2 M lithium sulfate at 18C using the hanging drop vapor diffusion method. They are incubated in the presence of 30% glycerol before being flash-frozen in liquid nitrogen. The crystals belong to trigonal space group P3(1)21 with a = b = 69.9 A and c = 117.2 A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, stable for storage in 10 mM K+/Hepes buffer (pH 7.5) or in 10 mM Tris buffer (pH 8.1) containing 10 mM KCl for several months
0C, pH 8.1, stored in 10 mM Tris buffer for several weeks without significant loss of activity
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D75A
no activity
N60A
significantly reduced activity
N60D
significantly reduced activity
D75A
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no activity
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N60A
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significantly reduced activity
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N60D
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significantly reduced activity
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D16A
significantly reduced activity
D61A
small but detectable level of catalytic activity
E14A
reduced activity
H52A
1000fold decrease in the kcat/Km is observed with the 4-hydroxyphenylacetyl-CoA, and a 100fold decrease in the kcat/Km value is observed with the 3-hydroxyphenylacetyl-CoA or 3,4-dihydroxyphenylacetyl-CoA
N15A
reduced activity
N46A
significantly reduced activity
N46Q/D61E
no activity