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Information on EC 6.2.1.37 - 3-hydroxybenzoate-CoA ligase and Organism(s) Thauera aromatica and UniProt Accession Q9AJS8

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.37 3-hydroxybenzoate-CoA ligase
IUBMB 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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This record set is specific for:
Thauera aromatica
UNIPROT: Q9AJS8
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Word Map
The taxonomic range for the selected organisms is: Thauera aromatica
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-hydroxybenzoate-coa ligase, 3-hydroxybenzoyl-coa synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxybenzoate-CoA/4-hydroxybenzoate-CoA ligase
bifunctional enzyme EC 6.2.1.27/6.2.1.37
3-hydroxybenzoate-coenzyme A ligase (AMP-forming)
-
3-hydroxybenzoyl coenzyme A synthetase
-
3-hydroxybenzoyl-CoA ligase
-
3-hydroxybenzoyl-CoA synthetase
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
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
?
-
NATURAL SUBSTRATE
NATURAL 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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.1
3-hydroxybenzoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
3-hydroxybenzoate
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
3-hydroxybenzoate
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.3
pH and temperature not specified in the publication
4.12
pH 7.8, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 hide
LITERATURE
7 - 9
pH 7.0: 20% of the activity at pH 9, pH 8.0: 65% of the activity at pH 9
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
3HBCL_THAAR
523
0
57607
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57500
x * 57500, SDS-PAGE
60000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 57500, SDS-PAGE
monomer
1 * 60000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the C-terminal His6-tagged protein in Escherichia coli BL21
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction during anaerobic growth with by 3-hydroxybenzoate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team