Information on EC 6.2.1.27 - 4-hydroxybenzoate-CoA ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
6.2.1.27
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxybenzoate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
-
-
-
ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
pathway
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
forming of carbon sulfur bonds
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-coumarate degradation (anaerobic)
-
Aminobenzoate degradation
-
Benzoate degradation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
phenol degradation II (anaerobic)
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate:CoA ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hydroxybenzoate-CoA/4-hydroxybenzoate-CoA ligase
Q9AJS8
bifunctional enzyme EC 6.2.1.27/6.2.1.37
4-hydroxybenzoate-CoA ligase
Q5P0J2
-
4-hydroxybenzoate-CoA ligase
Azoarcus sp. EbN1
Q5P0J2
-
-
4-hydroxybenzoate-CoA synthetase
-
-
-
-
4-hydroxybenzoate-coenzyme A ligase (AMP-forming)
-
-
-
-
4-hydroxybenzoyl coenzyme A synthetase
-
-
-
-
4-hydroxybenzoyl-CoA ligase
-
-
-
-
p-hydroxybenzoate-CoA ligase
-
-
p-hydroxybenzoate-CoA/benzoate-CoA ligase
-
-
synthetase, 4-hydroxybenzoyl coenzyme A
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
119699-80-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Azoarcus sp. EbN1
-
UniProt
Manually annotated by BRENDA team
strain K172
-
-
Manually annotated by BRENDA team
Pseudomonas sp. K172
strain K172
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4-aminobenzoate + CoA
AMP + 4-aminobenzoyl-CoA + diphosphate
show the reaction diagram
-
30% of the activity with 4-hydroxybenzoate
-
-
?
ATP + 4-fluorobenzoate + CoA
AMP + 4-fluorobenzoyl-CoA + diphosphate
show the reaction diagram
-
3.8% of the activity with 4-hydroxybenzoate
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q5P0J2
-
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
highly specific
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
anaerob
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
anaerob
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
anaerob
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37)
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q5P0J2
the bifunctional enzyme is also active with 3-hydroxybenzoate (at 44% of the activity with 4-hydroxybenzoate) (cf. EC 6.2.1.37)
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37). Activity with 4-hydroxybenzoate is 17% of the activity with 3-hydroxybenzoate
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37). Activity with 4-hydroxybenzoate is 69% compared to 3-hydroxybenzoate
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37). Activity with 4-hydroxybenzoate is 83% of the activity with 3-hydroxybenzoate
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37). kcat/Km for 4-hydroxybenzoate is 75% compared to the value for 3-hydroxybenzoate
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Azoarcus sp. EbN1
Q5P0J2
-, the bifunctional enzyme is also active with 3-hydroxybenzoate (at 44% of the activity with 4-hydroxybenzoate) (cf. EC 6.2.1.37)
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Pseudomonas sp. K172
-
highly specific, anaerob, initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + phenylacetate + CoA
AMP + phenylacetyl-CoA + diphosphate
show the reaction diagram
-
4.5% of the activity with 4-hydroxybenzoate
-
-
?
CTP + 4-hydroxybenzoate + CoA
CMP + 4-hydroxybenzoyl-CoA + diphosphate
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. K172
-
60% of the activity with ATP
-
-
?
additional information
?
-
-
not: benzoate, 3- or 2-hydroxybenzoate
-
-
-
additional information
?
-
-
no activity with 2-hydroxybenzoate, 2,3-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate and cinnamic acid
-
-
-
additional information
?
-
Q9AJS8
the enzyme shows low activity towards benzoate, 4-aminobenzoate, 3-aminobenzoate, 3-fluorobenzoate, 4-fluorobenzoate, 3-chlorobenzoate, and 4-chlorobenzoate. There is no activity with 3,4-dihydroxybenzoate, 2,3-dihydroxybenzoate, and 2-hydroxybenzoate as substrates
-
-
-
additional information
?
-
Pseudomonas sp. K172
-
not: benzoate, 3- or 2-hydroxybenzoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q5P0J2
-
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 3-hydroxybenzoate (cf. EC 6.2.1.37)
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Azoarcus sp. EbN1
Q5P0J2
-
-
-
?
ATP + 4-hydroxybenzoate + CoA
AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
Pseudomonas sp. K172
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-Dihydroxybenzoate
-
strong
2-hydroxy-4-methylbenzoate
-
strong
5,5'-dithiobis(2-nitrobenzoate)
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.037
-
4-hydroxybenzoate
-
pH 7.8, 37C
0.065
-
4-hydroxybenzoate
-
pH 7.8, 30C
0.34
-
4-hydroxybenzoate
-
pH and temperature not specified in the publication
0.077
-
ATP
-
pH 7.8, 37C
0.125
-
coenzyme A
-
pH 7.8, 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
24
-
4-hydroxybenzoate
-
pH and temperature not specified in the publication
30
-
4-hydroxybenzoate
-
pH 7.8, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
70
-
4-hydroxybenzoate
-
pH and temperature not specified in the publication
4552
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
-
2,4-Dihydroxybenzoate
-
pH 7.8, 37C
0.0014
-
2-hydroxy-4-methylbenzoate
-
pH 7.8, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
-
-
using benzoate as a substrate
0.0014
-
-
using p-hydroxybenzoate as a substrate
0.012
-
-
using p-cresol as a substrate
4.12
-
-
pH 7.8, 30C
4.8
-
Q5P0J2
pH and temperature not specified in the publication
37.3
-
-
-
additional information
-
-
no specific activity using acetate as a substrate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.2
8.5
-
-
9
-
-
or above. At a pH of above 9 the coupled spectrophotometric assay becomes limited due to instability of the substrates
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
pH 7.0: 20% of the activity at pH 9, pH 8.0: 65% of the activity at pH 9
7
9.5
-
50% of activity maximum at pH 7.0 and 9.5, almost no activity at pH 6.0 and 10.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
in the course of culture growth, the activity increases from day 6 and reaches maximum at day 10. This correlates well with the increases in the cell fresh weight and the xanthone content that starts also at day 6
Manually annotated by BRENDA team
-
comparison of enzyme activities grown anaerobically on various substrates
Manually annotated by BRENDA team
-
comparison of enzyme activities grown anaerobically on various substrates
Manually annotated by BRENDA team
Pseudomonas sp. K172
-
in the mid-exponential growth phase
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48000
-
-
gel filtration
50000
-
-
gel filtration
60000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q5P0J2
x * 54000, SDS-PAGE
?
-
x * 57500, SDS-PAGE
?
Azoarcus sp. EbN1
-
x * 54000, SDS-PAGE
-
monomer
-
1 * 48000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
Pseudomonas sp. K172
-
1 * 48000, SDS-PAGE
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxygen-sensitive during initial stages of purification, can be stabilized by adding DTT and 10% glycerol
-
648909
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Q5P0J2
DEAE-Sepharose chromatography, Reactive Green cross-linked agarose column chromatography, and Superdex 200 HiLoad 16/60 gel filtration
-
strain K172
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the gene product is expressed as a C-terminal His10-tagged protein in Escherichia coli BL21(DE3)
Q5P0J2
expression of the C-terminal His6-tagged protein in Escherichia coli BL21
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
induction during anaerobic growth with by 3-hydroxybenzoate
-