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Information on EC 6.2.1.37 - 3-hydroxybenzoate-CoA ligase
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6.2.1.37 3-hydroxybenzoate-CoA ligaseIUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-hydroxybenzoate-coa ligase, 3-hydroxybenzoyl-coa synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxybenzoate-CoA/4-hydroxybenzoate-CoA ligase
bifunctional enzyme EC 6.2.1.27/6.2.1.37
4-hydroxybenzoate-CoA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 3-hydroxybenzoate + CoA = AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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.
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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
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
the bifunctional enzyme is also active with 4-hydroxybenzoate, with 2.3fold higher activity compared to 3-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
the bifunctional enzyme is also active with 4-hydroxybenzoate, with 2.3fold higher activity compared to 3-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
-
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
the enzyme is involved in the biosynthesis of xanthones
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
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
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
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
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
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
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
-
-
?
additional information
?
-
-
no activity with 2-hydroxybenzoate, 2,3-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate and cinnamic acid
-
-
?
additional information
?
-
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
?
-
-
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
-
-
?
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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
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
the enzyme is involved in the biosynthesis of xanthones
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
-
the enzyme is involved in xanthone biosynthesis
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
the bifunctional enzyme is also active with 4-hydroxybenzoate (cf. EC 6.2.1.27)
-
-
?
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
the enzyme is involved in the anaerobic hydroxybenzoate metabolism
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
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+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
3-hydroxybenzoate
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
3-hydroxybenzoate
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
150
3-hydroxybenzoate
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
or above. At a pH of above 9 the coupled spectrophotometric assay becomes limited due to instability of the substrates
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pH RANGE
ORGANISM
UNIPROT
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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
brenda
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
brenda
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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). A0A1J5SK80_9ZZZZ
445
0
47409
TrEMBL
other Location (Reliability: 3)
A0A1J5RGF3_9ZZZZ
443
0
48048
TrEMBL
other Location (Reliability: 2)
A0A1J5S3P7_9ZZZZ
505
0
54703
TrEMBL
other Location (Reliability: 4)
A0A1J5S2U8_9ZZZZ
443
0
47867
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme could be stored frozen for several months without appreciable loss of activity
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the C-terminal His6-tagged protein in Escherichia coli BL21
the gene product is expressed as a C-terminal His10-tagged protein in Escherichia coli BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barillas, W.; Beerhues, L.
3-Hydroxybenzoate:coenzyme A ligase and 4-coumarate:coenzyme A ligase from cultured cells of Centaurium erythraea
Planta
202
112-116
1997
Centaurium erythraea
brenda
Schmidt, W.; Beerhues, L.
Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum
FEBS Lett.
420
143-146
1997
Hypericum androsaemum
brenda
Barillas, W.; Beerhues, L.
3-Hydroxybenzoate:coenzyme A ligase from cell cultures of Centaurium erythraea: isolation and characterization
Biol. Chem.
381
155-160
2000
Centaurium erythraea
brenda
Laempe, D.; Jahn, M.; Breese, K.; Schgger, H.; Fuchs, G.
Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica
J. Bacteriol.
183
968-979
2001
Thauera aromatica (Q9AJS8), Thauera aromatica
brenda
Ding, B.; Schmeling, S.; Fuchs, G.
Anaerobic metabolism of catechol by the denitrifying bacterium Thauera aromatica - a result of promiscuous enzymes and regulators?
J. Bacteriol.
190
1620-1630
2007
Azoarcus sp. (Q5P0J2), Thauera aromatica (Q9AJS8), Thauera aromatica, Azoarcus sp. EbN1 (Q5P0J2)
brenda
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Release 2023.1 (January 2023)
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