Information on EC 6.3.1.18 - gamma-glutamylanilide synthase

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The expected taxonomic range for this enzyme is: Acinetobacter

EC NUMBER
COMMENTARY hide
6.3.1.18
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RECOMMENDED NAME
GeneOntology No.
gamma-glutamylanilide synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + aniline = ADP + phosphate + N5-phenyl-L-glutamine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aniline degradation
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:aniline ligase (ADP-forming)
Requires Mg2+. The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the first step in the degradation of aniline. It can also accept chlorinated and methylated forms of aniline, preferrably in the o- and p-positions.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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 + L-glutamate + 2-chloroaniline
?
show the reaction diagram
ATP + L-glutamate + 2-methylaniline
?
show the reaction diagram
ATP + L-glutamate + 3-chloroaniline
?
show the reaction diagram
ATP + L-glutamate + 3-methylaniline
?
show the reaction diagram
ATP + L-glutamate + 4-chloroaniline
?
show the reaction diagram
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92% activity compared to aniline
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?
ATP + L-glutamate + 4-methylaniline
?
show the reaction diagram
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45% activity compared to aniline
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?
ATP + L-glutamate + aniline
ADP + phosphate + N5-phenyl-L-glutamine
show the reaction diagram
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 + L-glutamate + aniline
ADP + phosphate + N5-phenyl-L-glutamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required, 5 mM used in assay conditions
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
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6 * 55000, SDS-PAGE
350000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hi-Trap Q Sepharose column chromatography and Hi-Trap butyl FF column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain SO58
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