Information on EC 3.5.3.13 - formimidoylglutamate deiminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.3.13
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RECOMMENDED NAME
GeneOntology No.
formimidoylglutamate deiminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Histidine metabolism
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L-histidine degradation II
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histidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
N-formimidoyl-L-glutamate iminohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9054-85-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PA01
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Manually annotated by BRENDA team
ATCC 12633
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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
N-formimidoyl-L-glutamate + H2O
N-formyl-L-glutamate + NH3
show the reaction diagram
-
-
-
?
N-formimino-alpha-aminobutyric acid + H2O
N-formyl-alpha-aminobutyric acid + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-D-glutamate + H2O
N-formyl-D-glutamate + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-gamma-aminobutyric acid + H2O
N-formyl-gamma-aminobutyric acid + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-glycine + H2O
N-formyl-glycine + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-L-alanine + H2O
N-formyl-L-alanine + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-L-aspartate + H2O
N-formyl-L-aspartate + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-L-glutamate + H2O
N-formyl-L-glutamate + NH3
show the reaction diagram
N-formimino-L-glutamic acid + H2O
N-formyl-L-glutamic acid + NH3
show the reaction diagram
N-formimino-L-isoleucine + H2O
N-formyl-L-isoleucine + NH3
show the reaction diagram
-
pH 8.0, 30°C
-
-
?
N-formimino-L-leucine + H2O
N-formyl-L-leucine + NH3
show the reaction diagram
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pH 8.0, 30°C
-
-
?
N-formimino-L-methionine + H2O
N-formyl-L-methionine + NH3
show the reaction diagram
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pH 8.0, 30°C
-
-
?
N-formimino-L-phenylalanine + H2O
N-formyl-L-phenylalanine + NH3
show the reaction diagram
-
pH 8.0, 30°C
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-
?
N-formimino-L-tyrosine + H2O
N-formyl-L-tyrosine + NH3
show the reaction diagram
-
pH 8.0, 30°C
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-
?
N-formimino-L-valine + H2O
N-formyl-L-valine + NH3
show the reaction diagram
-
pH 8.0, 30°C
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-
?
N-guanidino-L-glutamate + H2O
?
show the reaction diagram
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pH 8.0, 30°C
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?
additional information
?
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formimino-L-aspartate and formiminoglycine are no substrates
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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
N-formimidoyl-L-glutamate + H2O
N-formyl-L-glutamate + NH3
show the reaction diagram
Q9HU77
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-
-
?
N-formimino-L-glutamate + H2O
N-formyl-L-glutamate + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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can replace Zn2+
Cu2+
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can replace Zn2+
Ni2+
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can replace Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dipicolinate
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zinc can be removed by dialysis against the metal chelator dipicolinate with the complete loss of catalytic activity
N-formimino-L-aspartate
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N-guanidino-L-glutamate
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N-guanidino-L-glutaric acid
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Tetranitromethane
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98% inhibition
additional information
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no inhibition by N-acetyl-L-glutamate, N-carbamoyl-L-glutamate, N-formyl-L-glutamate, N-formimino-alpha-aminobutyric acid and N-formimino-gamma-aminobutyric acid at concentrations up to 10 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
formiminoglutamate
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0.0012 - 19
N-formimino-L-glutamate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
N-formimino-D-glutamate
Pseudomonas aeruginosa
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pH 8.0, 30°C
0.005 - 31
N-formimino-L-glutamate
0.019
N-formimino-L-isoleucine
Pseudomonas aeruginosa
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pH 8.0, 30°C
0.01
N-formimino-L-methionine
Pseudomonas aeruginosa
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pH 8.0, 30°C
additional information
additional information
Pseudomonas aeruginosa
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less than 0.001/sec for the substrates N-guanidino-L-glutamate, N-formimino-alpha-aminobutyric acid, N-formimino-gamma-aminobutyric acid, N-formimino-L-alanine, N-formimino-L-aspartate, N-formimino-glycine, N-formimino-L-leucine, N-formimino-L-phenylalanine, N-formimino-L-tyrosine, N-formimino-L-valine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
N-formimino-L-aspartate
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pH 8.0, 30°C
0.89
N-guanidino-L-glutamate
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pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
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wild type PRS1, inducer N-formimino-L-glutamate
0.005
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wild type PRS1; wild type PRS1, inducer N-formyl-L-glutamate
0.015
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wild type PRS1, inducer urocanate
0.06
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strain PS15(hutU)
0.066
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wild type PRS1, inducer histidine
0.086
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strain LH13(hutC)
0.09
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strain LH12(hutC)
0.093
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strain LH11(hutC)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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2 * 45000, sedimentation equilibrium experiment at 20000 rpm
48000
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2 * 48000, sedimentation equilibrium experiment at 22000 rpm
49000
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2 * 49000, SDS-PAGE, gel filtration
50000
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2 * 50000, SDS-PAGE
53000
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2 * 53000, SDS-PAGE
96000
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gel filtration, sedimentation equilibrium experiment at 6000 rpm
100000
108000
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gel filtration, sedimentation equilibrium experiment at 12000 rpm
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in the presence of the inhibitors N-formimino-L-aspartate and N-guanidino-L-glutaric acid, hanging drop vapor diffusion method, using
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C gradually loses activity over a period of several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, High Load 26/60 Superdex 200 gel filtration, and Resource Q anion exchange column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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pMCl, entire group of hut genes from P. putida ATCC 12633 cloned into Escherichia coli , hutF encodes FIGLU iminohydrolase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E235A
-
lower activity compared to the wild type enzyme
E235Q
-
lower activity compared to the wild type enzyme
H269A
-
about 5fold lower activity compared to the wild type enzyme
H269C
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about 5fold lower activity compared to the wild type enzyme
H269N
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about 5fold lower activity compared to the wild type enzyme
E235A
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lower activity compared to the wild type enzyme
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E235Q
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lower activity compared to the wild type enzyme
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H269A
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about 5fold lower activity compared to the wild type enzyme
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H269C
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about 5fold lower activity compared to the wild type enzyme
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H269N
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about 5fold lower activity compared to the wild type enzyme
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