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Information on EC 3.5.2.7 - imidazolonepropionase
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3.5.2.7 imidazolonepropionaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
4-imidazolone-5-propanoate amidohydrolase, HutI, imidazolone-5-propanoate hydrolase, Imidazolone-5-propionate hydrolase, imidazolonepropionase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-imidazolone-5-propanoate amidohydrolase
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-
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HutI
Imidazolone-5-propionate hydrolase
imidazolonepropionase
Imidazolone-5-propionate hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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
9024-91-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
N-formimidoyl-L-glutamate + H+
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?
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
N-formimidoyl-L-glutamate + H+
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
?
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
-
r
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
-
ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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ir
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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-
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?
4(5)-imidazolone-5(4)-propionic acid + H2O
N-formimino-L-glutamate
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ir
additional information
?
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analysis of substrate specificity and catalytic mechanism of imidazolonepropionase considering the four isomers of (S)- and (R)-enantiomers of 4-imidazolone-5-propionic acid (SIPA-1, SIPA-2, RIPA-1 and RIPA-2), overview. SIPA-1 is suggested to be the most favorable substrate for HutI, whereas the hydrolytic cleavage of SIPA-2 may require a preliminary isomerization to SIPA-1
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additional information
?
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analysis of substrate specificity and catalytic mechanism of imidazolonepropionase considering the four isomers of (S)- and (R)-enantiomers of 4-imidazolone-5-propionic acid (SIPA-1, SIPA-2, RIPA-1 and RIPA-2), overview. SIPA-1 is suggested to be the most favorable substrate for HutI, whereas the hydrolytic cleavage of SIPA-2 may require a preliminary isomerization to SIPA-1
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additional information
?
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analysis of substrate specificity and catalytic mechanism of imidazolonepropionase considering the four isomers of (S)- and (R)-enantiomers of 4-imidazolone-5-propionic acid (SIPA-1, SIPA-2, RIPA-1 and RIPA-2), overview. SIPA-1 is suggested to be the most favorable substrate for HutI, whereas the hydrolytic cleavage of SIPA-2 may require a preliminary isomerization to SIPA-1
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
N-formimidoyl-L-glutamate + H+
-
-
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?
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O
N-formimidoyl-L-glutamate + H+
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-
-
?
4(5)-imidazolone-5(4)-propionic acid + H2O
?
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
0.1
4(5)-imidazolone-5(4)-propionic acid
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additional information
additional information
determination of reaction thermodynamics
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additional information
additional information
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determination of reaction thermodynamics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
additional information
metabolism
imidazolonepropionase (HutI) catalyzes the hydrolytic cleavage of carbon-nitrogen bond in 4-imidazolone-5-propionic acid (IPA) to yield L-formiminoglutamic acid, which is the third step in the universal histidine degradation pathway
metabolism
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imidazolonepropionase (HutI) catalyzes the hydrolytic cleavage of carbon-nitrogen bond in 4-imidazolone-5-propionic acid (IPA) to yield L-formiminoglutamic acid, which is the third step in the universal histidine degradation pathway
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additional information
catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
additional information
-
catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
additional information
-
catalytic mechanism, modeling, optimized structures of transition states and intermediates, combined quantum mechanics and molecular mechanics (QM/MM) calculations and modeling, overview. Activation of hydrolytic water (a zinc-bound water) is performed by residue E252 via a bridging water molecule, which occurs before binding of the substrate. After the substrate binding, this activation channel is blocked by the substrate, and the other two residues (D324 and H272) cannot act as the general base to activate the hydrolytic water. For the two (S)-enantiomers of IPA, HutI can specifically convert one isomer of (S)-enantiomer (SIPA-1) to l-formiminoglutamic acid
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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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
sitting drop vapour diffusion method with 25% (w/v) PEG 3350, 0.1M Bis-Tris pH 5.5, and 0.2 M MgCl2
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Consevage, M.W.; Porter, R.D.; Phillips, A.T.
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida
brenda
Kendrick, K.E.; Wheelis, M.L.
Histidine dissimilation in Streptomyces coelicolor
J. Gen. Microbiol.
128
2029-2040
1982
Streptomyces coelicolor
brenda
Snyder, S.H.
Imidazolonepropionic acid hydrolase (Rat liver)
Methods Enzymol.
17B
92-95
1971
Rattus norvegicus
-
brenda
Magasanik, B.; Kaminskas, E.; Kimhi, Y.
Imidazolonepropionic acid hydrolase (Bacillus subtilis)
Methods Enzymol.
17B
55-57
1971
Bacillus subtilis
-
brenda
Holm, L.; Sander, C.
An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
Proteins Struct. Funct. Genet.
28
72-82
1997
Caenorhabditis elegans
brenda
Smith, G.R.; Halpern, Y.S.; Magasanik, B.
Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase
J. Biol. Chem.
246
3320-3329
1971
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Snyder, S.H.; Silva, O.L.; Kies, M.W.
The mammalian metabolism of L-histidine: IV. Purification and properties of imidazolone propionic acid hydrolase
J. Biol. Chem.
236
2996-2998
1961
Rattus norvegicus
brenda
Rao, D.R.; Greenberg, D.M.
Studies on the enzymic decomposition of urocanic acid
J. Biol. Chem.
236
1758-1763
1961
Klebsiella aerogenes, Bos taurus, Cavia porcellus, Clostridium tetanomorphum, Ovis aries, Pseudomonas fluorescens, Rattus norvegicus, Sus scrofa
brenda
Yu, Y.; Li, L.; Zheng, X.; Liang, Y.; Su, X.
Protein preparation, crystallization and preliminary x-ray analysis of imidazolonepropionase from Bacillus subtilis
Biochim. Biophys. Acta
1764
153-156
2006
Bacillus subtilis (P42084), Bacillus subtilis
brenda
Tyagi, R.; Eswaramoorthy, S.; Burley, S.K.; Raushel, F.M.; Swaminathan, S.
A common catalytic mechanism for proteins of the HutI family
Biochemistry
47
5608-5615
2008
Agrobacterium tumefaciens (Q8U8Z6), Agrobacterium tumefaciens
brenda
Yu, Y.; Liang, Y.H.; Brostromer, E.; Quan, J.M.; Panjikar, S.; Dong, Y.H.; Su, X.D.
A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis
J. Biol. Chem.
281
36929-36936
2006
Bacillus subtilis (P42084), Bacillus subtilis
brenda
Yang, F.; Chu, W.; Yu, M.; Wang, Y.; Ma, S.; Dong, Y.; Wu, Z.
Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations
J. Synchrotron Radiat.
15
129-133
2008
Bacillus subtilis (P42084), Bacillus subtilis
brenda
Tyagi, R.; Kumaran, D.; Burley, S.K.; Swaminathan, S.
X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution
Proteins Struct. Funct. Bioinform.
69
652-658
2007
Agrobacterium tumefaciens (Q8U8Z6), Agrobacterium tumefaciens
brenda
Su, H.; Sheng, X.; Liu, Y.
Exploring the substrate specificity and catalytic mechanism of imidazolonepropionase (HutI) from Bacillus subtilis
Phys. Chem. Chem. Phys.
18
27928-27938
2016
Bacillus subtilis (P42084), Bacillus subtilis, Bacillus subtilis 168 (P42084)
brenda
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