Information on EC 3.5.3.8 - formimidoylglutamase

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

EC NUMBER
COMMENTARY hide
3.5.3.8
-
RECOMMENDED NAME
GeneOntology No.
formimidoylglutamase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-N bond of an amidino group
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Histidine metabolism
-
-
L-histidine degradation I
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Metabolic pathways
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histidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
N-formimidoyl-L-glutamate formimidoylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-92-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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UniProt
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
N-formimidoyl-L-glutamate + H2O
formate + ammonium + glutamate
show the reaction diagram
-
-
-
-
?
N-formimidoyl-L-glutamate + H2O
L-glutamate + formamide
show the reaction diagram
additional information
?
-
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
N-formimidoyl-L-glutamate + H2O
formate + ammonium + glutamate
show the reaction diagram
-
-
-
-
?
N-formimidoyl-L-glutamate + H2O
L-glutamate + formamide
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
tetrahydrofolate
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetyl-L-glutamate
-
competitive inhibitor
N-formyl-L-aspartate
-
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9 - 530
N-formimidoyl-L-glutamate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 200
N-formimidoyl-L-glutamate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052 - 5.2
N-formimidoyl-L-glutamate
6712
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
gel filtration
220000
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ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 50000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 25% PEG (w/v) 3350, 0.1 M sodium acetate (pH 4.6)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
90 min, 32% loss in activity
54
-
15 min, 67% loss in activity
80
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15 min, totally inactivated
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, 10 days, 75% in activity are lost
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial purification
Talon column chromatography and Q-HP anion exchange column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N114H
the mutant exhibits 35% loss of catalytic efficiency compared to the wild type enzyme
R144A
the mutant exhibits 99.3% loss of catalytic efficiency compared to the wild type enzyme
R144E
the mutant exhibits 99.9% loss of catalytic efficiency compared to the wild type enzyme
R144K
the mutant exhibits 77% loss of catalytic efficiency compared to the wild type enzyme
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