Information on EC 6.2.1.37 - 3-hydroxybenzoate-CoA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY
6.2.1.37
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxybenzoate-CoA ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + 3-hydroxybenzoate + CoA = AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
tetrahydroxyxanthone biosynthesis (from 3-hydroxybenzoate)
-
SYSTEMATIC NAME
IUBMB Comments
3-hydroxybenzoate:CoA ligase (AMP-forming)
The enzyme works equally well with 4-hydroxybenzoate but 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.
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
3-hydroxybenzoateŚcoenzyme A ligase (AMP-forming)
Q9AJS8
-
3-hydroxybenzoyl coenzyme A synthetase
Q9AJS8
-
3-hydroxybenzoyl-CoA ligase
Q9AJS8
-
3-hydroxybenzoyl-CoA synthetase
Q9AJS8
-
4-hydroxybenzoate-CoA ligase
Q5P0J2
-
4-hydroxybenzoate-CoA ligase
Azoarcus sp. EbN1
Q5P0J2
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Azoarcus sp. EbN1
-
UniProt
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 + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8, -
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in the biosynthesis of xanthones
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27). Activity with 4-hydroxybenzoate is 17% of the activity with 3-hydroxybenzoate
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27). Activity with 4-hydroxybenzoate is 69% compared to 3-hydroxybenzoate
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8, -
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27). Activity with 4-hydroxybenzoate is 83% of the activity with 3-hydroxybenzoate
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27). kcat/Km for 4-hydroxybenzoate is 75% compared to the value for 3-hydroxybenzoate
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
Azoarcus sp., Azoarcus sp. EbN1
Q5P0J2
the bifunctional enzyme is also active with 4-hydroxybenzoate, with 2.3fold higher activity compared to 3-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
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
-
-
-
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 + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
Q9AJS8, -
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in the biosynthesis of xanthones
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
-
the enzyme is involved in xanthone biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
strictly dependent on Mg2+ or Mn2+ ions, with concentrations of 0.5 mM leading to maximum activity. No enzyme activity was found in the presence of Ca2+
Mn2+
-
strictly dependent on Mg2+ or Mn2+ ions, with concentrations of 0.5 mM leading to maximum activity. No enzyme activity was found in the presence of Ca2+
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0147
-
3-Hydroxybenzoate
-
pH 7.5, 35░C
0.06
-
3-Hydroxybenzoate
-
pH 7.8, 30░C
0.1
-
3-Hydroxybenzoate
-
pH and temperature not specified in the publication
0.229
-
ATP
-
pH 7.5, 35░C
0.0085
-
CoA
-
pH 7.5, 35░C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15
-
3-Hydroxybenzoate
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
150
-
3-Hydroxybenzoate
-
pH and temperature not specified in the publication
3769
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.12
-
-
pH 7.8, 30░C
14.3
-
-
pH and temperature not specified in the publication
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
6.5
8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 50% of maximal activity
7
9
-
pH 7.0: 20% of the activity at pH 9, pH 8.0: 65% of the activity at pH 9
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
3-hydroxybenzoate-CoA ligase is detected not only in 3-hydroxybenzoate-grown cells but also in catechol- and protocatechuate-grown cells. The enzyme is not detected in phenol-, 4-hydroxybenzoate-, and benzoate-grown cells
Manually annotated by BRENDA team
-
in the course of culture growth, the activities of both enzymes increase from day 6 and reached maxima 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
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
gel filtration
60000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
two polypeptides of 41500 Da and 40500 Da are detected by SDS-PAGE, difference in their apparent molecular masses can not be attributed to glycosylation
?
Q5P0J2
x * 53694, calculated from sequence; x * 54000, SDS-PAGE
?
-
x * 57500, SDS-PAGE
?
Azoarcus sp. EbN1
-
x * 53694, calculated from sequence; x * 54000, SDS-PAGE
-
monomer
-
1 * 60000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol, 5% does not affect enzyme stability
-
the enzyme could be stored frozen for several months without appreciable loss of activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Glycerol
-
5%, does not affect enzyme stability
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4░C, crude extracts prepared with 0.1 M potassium phosphate buffer, pH 7.5, complete loss of activity within 24 h
-
the enzyme could be stored frozen for several months without appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Q5P0J2
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
-