Information on EC 3.5.2.7 - imidazolonepropionase

for references in articles please use BRENDA:EC3.5.2.7
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
3.5.2.7
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RECOMMENDED NAME
GeneOntology No.
imidazolonepropionase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-histidine degradation I
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L-histidine degradation II
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L-histidine degradation III
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L-histidine degradation VI
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histidine metabolism
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Histidine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-91-3
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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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Manually annotated by BRENDA team
grown on histidine
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Manually annotated by BRENDA team
grown on histidine
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
grown on histidine
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4(5)-imidazolone-5(4)-propionic acid + H2O
?
show the reaction diagram
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
show the reaction diagram
imidazole-4-acetic acid + H2O
?
show the reaction diagram
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-
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-
?
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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(5)-imidazolone-5(4)-propionic acid + H2O
?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(2,5-dioxoimidazolidin-4-yl)propionic acid
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p-chloromercuribenzoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
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reduced, partially reversed inhibition of the enzyme by p-chloromercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 1.54
4(5)-imidazolone-5(4)-propionic acid
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.12
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streptomycin-treated extract of Bacillus subtilis, not purified
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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around pH 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240);
Agrobacterium fabrum (strain C58 / ATCC 33970);
Bacillus subtilis (strain 168);
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
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gel filtration
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apoenzyme crystals for HutI are obtained by the sitting drop vapour diffusion method with 1.8 M triammonium citrate (pH 7.0) and 25% (w/v) PEG 3350, 0.1 M Bis-Tris (pH 5.5), and 0.2 M MgCl2, N-formimino-L-glutamate is cocrystallized with HutI via hanging drop vapor diffusion at 20°C against a reservoir solution containing 25% (w/v) PEG 3350, 0.1 M Bis-Tris (pH 5.5), and 0.2 M MgCl2
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sitting drop vapour diffusion method with 25% (w/v) PEG 3350, 0.1M Bis-Tris pH 5.5, and 0.2 M MgCl2
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2.0 A resolution
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co-crystallization with imidazole-4-acetic acid sodium in 20% (w/v) polyethylene glycol 4000, 0.1 M Tris-HCl, pH 7.5, 0.2 M sodium acetate, and 2% (w/v) benzamidine hydrochloride
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 h, 50% loss of activity, stabilized by addition of MgCl2
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.2.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)