Information on EC 3.5.1.68 - N-formylglutamate deformylase

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

EC NUMBER
COMMENTARY hide
3.5.1.68
-
RECOMMENDED NAME
GeneOntology No.
N-formylglutamate deformylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formyl-L-glutamate + H2O = formate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of linear amides
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
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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-formyl-L-glutamate amidohydrolase
The animal enzyme also acts on beta-citryl-L-glutamate and beta-citryl-L-glutamine.
CAS REGISTRY NUMBER
COMMENTARY hide
113356-24-4
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88414-88-4
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97286-12-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pseudomonas spp.
Wistar
-
-
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
beta-citryl-L-glutamate + H2O
citrate + L-glutamate
show the reaction diagram
beta-citryl-L-glutamine + H2O
citrate + L-glutamine
show the reaction diagram
N-acetyl-alpha-L-aspartylglutamate + H2O
acetate + alpha-L-aspartylglutamate
show the reaction diagram
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poor substrate
-
-
?
N-acetyl-L-aspartate + H2O
acetate + L-aspartate
show the reaction diagram
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poor substrate
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
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poor substrate
-
-
?
N-formyl-L-glutamate + H2O
formate + L-glutamate
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-formyl-L-glutamate + H2O
formate + L-glutamate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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5 mM: high activation
Co2+
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activation, most effective, 0.8 mM: 4fold activation
Divalent metal ions
MnCl2
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5 mM: most effective activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenine
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1 mM: about 30% inhibition
ADP
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0.1 mM: about 30% inhibition, 1 mM: about 90% inhibition
citrate
CuSO4
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5 mM
dithiothreitol
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5 mM: very slight inhibition
Fe2+
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slight inhibition above 0.1 mM, activation below 0.1 mM
FeCl3
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5 mM: strong inhibition
FeSO4
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5 mM
GDP
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1 mM: about 62% inhibition
glutamate
guanine
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0.1 mM: about 11% inhibition, 1 mM: about 4% inhibition
L-Quisqualate
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0.1 mM: 80% inhibition, 1 mM: 96% inhibition; non-competitive potent inhibitor
MgCl2
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5 mM
N-acetyl-L-glutamate
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kinetics, competitive inhibition, Ki: 6 mM
N-acetyl-L-glutamine
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slight inhibition
N-formyl-L-aspartate
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kinetics, competitive inhibition, Ki: 9 mM
NiCl2
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5 mM
nucleotides
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strong inhibition
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phosphate
S-adenosyl-L-methionine
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0.1 mM: about 6% inhibition, 1 mM: about 30% inhibition
ZnCl2
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5 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histidine
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induction and activation
Lubrol Px
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enzyme solubilized, activation
N-formyl-L-glutamate
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induction and activation
Triton X-100
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enzyme solubilized, activation
Urocanate
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induction and activation
additional information
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sulfhydryl reagent not required
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 0.0088
beta-Citryl-L-glutamate
14
N-formyl-L-glutamate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
N-acetyl-L-glutamate
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kinetics, competitive inhibition
9
N-formyl-L-aspartate
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kinetics, competitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
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in the presence of 5 mM substrate, N-formyl-L-glutamate, and 0.8 mM CoCl2, 30°C
380
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calculated specific activity, with saturating substrate
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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in the presence of Mn2+
7 - 8
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maximally active at
7.5
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100 mM potassium phosphate buffer; assay at
additional information
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pI of about pH 4.3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.5
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more than 65% of maximal activity between pH 6.6 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low activity
Manually annotated by BRENDA team
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moderate activity
Manually annotated by BRENDA team
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high activity, about 40% of the level in testis
Manually annotated by BRENDA team
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low activity
Manually annotated by BRENDA team
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low activity
Manually annotated by BRENDA team
additional information
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tissue distribution, highest activity in testes and lung
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
present in soluble fractions
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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1 * 50000, SDS-PAGE
52000
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gel filtration
350000
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PAGE, after digestion with N-glycosidase F
380000
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gel filtration
420000
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PAGE, before digestion with N-glycosidase F
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 50000, SDS-PAGE
multimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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2 min: 5% loss of activity, 5 min: 10% loss of activity
100
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boiling, 2 min: 100% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from recombinant Escherichia coli strain RDP145, pLH4
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partial; solubilized by 0.5% Lubrol PX, most effective detergent
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solubilized by 0.5% Lubrol PX, most effective detergent
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli RDP210
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hutG, formylglutamate amidohydrolase gene, expressed in Escherichia coli RDP145; hutG , formylglutamate amidohydrolase gene, subcloned on a multicopy plasmid in Escherichia coli
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