Information on EC 3.5.1.B18 - 4-aminobenzoylglutamate hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.B18
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
4-aminobenzoylglutamate hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of C-terminal glutamate from 4-aminobenzoylglutamate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
N-(4-aminobenzoyl)-L-glutamate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
220181-59-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
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-
Manually annotated by BRENDA team
cv. Laxton’s Progress 9
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-
Manually annotated by BRENDA team
cv. Micro-Tom
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
cv. NK508
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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
4-aminobenzoylglutamate + H2O
4-aminobenzoic acid + L-glutamate
show the reaction diagram
folic acid + H2O
pteroic acid + L-glutamate
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
4-aminobenzoylglutamate + H2O
4-aminobenzoic acid + L-glutamate
show the reaction diagram
folic acid + H2O
pteroic acid + L-glutamate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
54% activation at 0.1 mM, metalloenzyme
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
25% inhibition at 0.1 mM
8-Hydroxyquinoline-5-sulfonate
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complete inhibition at 1 mM
Cu2+
-
complete inhibition
DTNB
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25% inhibition at 1 mM
DTT
-
53% inhibition at 1 mM
EDTA
-
21% inhibition at 1 mM
folate
-
substrate inhibition, competitive
Hg2+
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complete inhibition
N,N,N',N'-tetrakis[2-pyridylmethyl]ethylenediamine
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i.e. TPEN, 53% inhibition at 0.1 mM
Pepstatin
-
25% inhibition at 0.0015 mM
PMSF
-
15% inhibition at 1 mM
additional information
-
the enzyme activity is fairly insensitive to serine, cysteine, and aspartic reagents, but is inhibited by metal chelators
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
4-aminobenzoylglutamate
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pH 7.4, 37°C
additional information
additional information
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kinetics
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052
folic acid
Arabidopsis thaliana
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pH 7.4, 37°C, versus 4-aminobenzoylglutamate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00029
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purified enzyme from roots
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.3
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50% of maximal activity at pH 6.5 and pH 8.3, pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity in chloroplasts, the enzyme is probably also partially located in vacuoles
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
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main peak, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from 268fold leaves and 86fold from roots by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, followed by gel filtration, activity loss during purification exceeds 95%
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