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
LITERATURE
ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
pathway
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
forming of carbon sulfur bonds
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-coumarate degradation (anaerobic)
-
-
Aminobenzoate degradation
-
-
Benzoate degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
phenol degradation
-
-
phenol degradation II (anaerobic)
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate:CoA ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4-hydroxybenzoate-CoA synthetase
-
-
-
-
4-hydroxybenzoate-coenzyme A ligase (AMP-forming)
-
-
-
-
4-hydroxybenzoyl coenzyme A synthetase
-
-
-
-
4-hydroxybenzoyl-CoA ligase
-
-
-
-
synthetase, 4-hydroxybenzoyl coenzyme A
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
119699-80-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
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
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
COMMENTARY
LITERATURE
IMAGE
2,4-Dihydroxybenzoate
-
strong
2-hydroxy-4-methylbenzoate
-
strong
5,5'-dithiobis(2-nitrobenzoate)
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70
4-hydroxybenzoate
-
pH and temperature not specified in the publication
365
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
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
additional information
-
no specific activity using acetate as a substrate
pH OPTIMUM
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
-
gel filtration
648909
50000
-
gel filtration
713330
60000
-
gel filtration
712273
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q5P0J2
x * 54000, SDS-PAGE
?
-
x * 57500, SDS-PAGE
?
Azoarcus sp. EbN1
-
x * 54000, SDS-PAGE
-
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
monomer
Pseudomonas sp. K172
-
1 * 48000, SDS-PAGE
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen-sensitive during initial stages of purification, can be stabilized by adding DTT and 10% glycerol
-
648909
Purification/COMMENTARY
ORGANISM
UNIPROT
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
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
LITERATURE
induction during anaerobic growth with by 3-hydroxybenzoate
-