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Information on EC 6.2.1.27 - 4-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
                6.2.1.27 4-hydroxybenzoate-CoA ligase
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This record set is specific for:
Thauera aromatica
UNIPROT: Q9AJS8 not found.
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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
4-hydroxybenzoate-coa ligase, 4-hydroxybenzoyl-coa ligase, p-hydroxybenzoate-coa ligase, 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
4-hydroxybenzoate-CoA synthetase
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-
-
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4-hydroxybenzoate-coenzyme A ligase (AMP-forming)
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-
-
-
4-hydroxybenzoyl coenzyme A synthetase
-
-
-
-
4-hydroxybenzoyl-CoA ligase
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-
-
-
synthetase, 4-hydroxybenzoyl coenzyme A
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA
show the reaction diagram
pathway
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
119699-80-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
initial step of anaerobic 4-hydroxybenzoate degradation
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.34
4-hydroxybenzoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24
4-hydroxybenzoate
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70
4-hydroxybenzoate
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
comparison of enzyme activities grown anaerobically on various substrates
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
Heider, J.; Boll, M.; Breese, K.; Breinig, S.; Ebenau-Jehle, C.; Feil, U.; Gad'on, N.; Laempe, D.; Leuthner, B.; Mohamed, M.E.S.; Schneider, S.; Burchhardt, G.; Fuchs, G.
Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
170
120-131
1998
Thauera aromatica
Manually annotated by BRENDA team
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)
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), Azoarcus sp. EbN1 (Q5P0J2)
Manually annotated by BRENDA team