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Information on EC 3.1.2.25 - phenylacetyl-CoA hydrolase
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3.1.2.25 phenylacetyl-CoA hydrolaseIUBMB Comments
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
More, PaaI, PaaI thioesterase, phenylacetyl coenzyme A hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PaaI
PaaI thioesterase
additional information
additional information
-
an enzyme preparation of phenylacetyl-CoA:acceptor oxidoreductase, EC 1.17.5.1, catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1
additional information
-
an enzyme preparation of phenylacetyl-CoA:acceptor oxidoreductase, EC 1.17.5.1, catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, may be an additional membrane-bound enzyme or more likely one of the subunits of phenylacetyl-CoA:acceptor oxidoreductase is responsible for the hydrolysis of phenylglyoxylyl-CoA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA
first step
-
-
-
phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
phenylglyoxylyl-CoA hydrolase
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
210756-43-7
cf. 1.17.5.1
57219-72-4
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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
arachidonyl-CoA + H2O
arachidonate + CoA
very low activity
-
-
?
decanoyl-CoA + H2O
decanoate + CoA
highest activity
-
-
?
dodecanoyl-CoA + H2O
dodecanoate + CoA
high activity
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
hydrolyzes p-nitrophenyl acetate at the same rate as phenylacetyl-CoA or phenoxyacetylglycine
-
?
phenoxyacetyl-CoA + H2O
phenoxyacetate + CoA
-
approximately 5fold higher activity than with phenylacetyl-CoA
-
?
phenoxyacetylglycine + H2O
?
-
hydrolyzes phenoxyacetylglycine at the same rate as phenylacetyl-CoA or p-nitrophenyl acetate
-
?
acetyl-CoA + H2O
acetate + CoA
very low activity
-
-
?
butyryl-CoA + H2O
butanoate + CoA
low activity
-
-
?
myristoyl-CoA + H2O
myristate + CoA
very low activity
-
-
?
myristoyl-CoA + H2O
myristate + CoA
very low activity
-
-
?
phenylacetyl-CoA + H2O
phenylacetate + CoA
-
hydrolyzes phenylacetyl-CoA at the same rate as p-nitrophenyl acetate or phenoxyacetylglycine, approximately 5fold lower activity as with phenoxyacetyl-CoA
-
?
phenylacetyl-CoA + H2O
phenylacetate + CoA
low activity. The wild type enzyme displays a greater activity for phenylacetyl-CoA than very short and long chain saturated fatty acyl-CoA substrates
-
-
?
phenylglyoxylyl-CoA + H2O
phenylglyoxylate + CoA
-
hydrolytic release of coenzyme A from phenylglyoxylyl-CoA
-
?
phenylglyoxylyl-CoA + H2O
phenylglyoxylate + CoA
-
involved in anaerobic metabolism of phenylalanine, catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1
-
?
additional information
?
-
no activity with malonyl-CoA, palmitoyl-CoA, and stearoyl-CoA
-
-
?
additional information
?
-
-
no activity with malonyl-CoA, palmitoyl-CoA, and stearoyl-CoA
-
-
?
additional information
?
-
no activity with malonyl-CoA, palmitoyl-CoA, and stearoyl-CoA
-
-
?
additional information
?
-
-
catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1
-
?
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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
phenylglyoxylyl-CoA + H2O
phenylglyoxylate + CoA
-
involved in anaerobic metabolism of phenylalanine, catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1
-
?
additional information
?
-
-
catalyzes the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.5
phenylacetyl-CoA
wild type enzyme, at pH 7.6 and 21°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
72
phenylacetyl-CoA
wild type enzyme, at pH 7.6 and 21°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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). A0A0M3KL39_STRPN
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
137
0
15217
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Crystals of wild type enzyme and mutants N37A, D52A, and T68A are obtained in conditions composed of 200 mM ammonium tartrate dibasic, 20% (w/v) PEG 3350, 100 mM Tris, pH 7.5; 200 mM lithium sulfate, 100 mM Tris-HCl, 30% (w/v) PEG 4000, 200 mM magnesium chloride, PEG 400, 100 mM HEPES, pH 7.5; 200 mM magnesium chloride, 14% (w/v) PEG 3350, 100 mM Tris, pH 6.0, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T68A
the mutant shows a marked reduction in activity compared to the wild type enzyme
T68A
-
the mutant shows a marked reduction in activity compared to the wild type enzyme
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap affinity column chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rhee, S.K.; Fuchs, G.
Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica
Eur. J. Biochem.
262
507-515
1999
Thauera aromatica
brenda
Schneider, S.; Fuchs, G.
Phenylacetyl-CoA:acceptor oxidoreductase, a new a-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica
Arch. Microbiol.
169
509-516
1998
Thauera aromatica
brenda
Brian, S.
Phenylacetyl coenzyme A hydrolase
Methods Enzymol.
43
482-487
1975
Penicillium chrysogenum
brenda
Khandokar, Y.; Srivastava, P.; Sarker, S.; Swarbrick, C.; Aragao, D.; Cowieson, N.; Forwood, J.
Structural and functional characterization of the PaaI thioesterase from Streptococcus pneumoniae reveals a dual specificity for phenylacetyl-CoA and medium-chain fatty Acyl-CoAs and a novel CoA-induced fit mechanism
J. Biol. Chem.
291
1866-1876
2016
Streptococcus pneumoniae (A0A0M3KL39), Streptococcus pneumoniae, Streptococcus pneumoniae ATCC BAA-334 (A0A0M3KL39)
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