Information on EC 6.2.1.37 - 3-hydroxybenzoate-CoA ligase

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

EC NUMBER
COMMENTARY hide
6.2.1.37
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybenzoate-CoA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 3-hydroxybenzoate + CoA = AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrahydroxyxanthone biosynthesis (from 3-hydroxybenzoate)
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 3-hydroxybenzoate + CoA
AMP + diphosphate + 3-hydroxybenzoyl-CoA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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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+
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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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0147 - 0.1
3-hydroxybenzoate
0.229
ATP
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pH 7.5, 35░C
0.0085
CoA
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pH 7.5, 35░C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
3-hydroxybenzoate
Thauera aromatica
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pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
3-hydroxybenzoate
Thauera aromatica
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pH and temperature not specified in the publication
1002
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.12
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pH 7.8, 30░C
14.3
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pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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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 hide
LITERATURE
6.5 - 8.5
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pH 6.5: about 50% of maximal activity, pH 8.5: about 50% of maximal activity
7 - 9
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pH 7.0: 20% of the activity at pH 9, pH 8.0: 65% of the activity at pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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gel filtration
60000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 60000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, 5% does not affect enzyme stability
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the enzyme could be stored frozen for several months without appreciable loss of activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glycerol
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5%, does not affect enzyme stability
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
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the enzyme could be stored frozen for several months without appreciable loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the C-terminal His6-tagged protein in Escherichia coli BL21
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the gene product is expressed as a C-terminal His10-tagged protein in Escherichia coli BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction during anaerobic growth with by 3-hydroxybenzoate
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