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Information on EC 3.5.1.32 - hippurate hydrolase
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3.5.1.32 hippurate hydrolaseIUBMB Comments
Acts on various N-benzoylamino acids.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
Benzoylglycine amidohydrolase, hippurate hydrolase, hippuricase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hippurate + H2O = benzoate + glycine
residues Asp76, Aps104, Glu134, Glu135, His161 and His356 are involved in zinc-binding and enzyme catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
N-benzoylamino-acid amidohydrolase
Acts on various N-benzoylamino acids.
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CAS REGISTRY NUMBER
COMMENTARY
37278-43-6
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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
4-acetyl-N-benzoyl-L-alanine + H2O
4-acetylbenzoic acid + L-alanine
-
low activity
-
?
4-acetyl-N-benzoylglycine + H2O
4-acetylbenzoic acid + glycine
-
-
-
?
4-chloro-N-benzoyl-L-alanine + H2O
4-chlorobenzoic acid + L-alanine
-
-
-
?
4-chloro-N-benzoylglycine + H2O
4-chlorobenzoic acid + glycine
-
-
-
?
4-hydroxy-N-benzoyl-L-alanine
4-hydroxybenzoic acid + L-alanine
-
low activity
-
?
4-hydroxy-N-benzoylglycine + H2O
4-hydroxybenzoic acid + glycine
-
-
-
?
4-hydroxy-N-benzoylglycine-L-histidyl-L-leucine + H2O
4-hydroxybenzoic acid + L-histidyl-L-leucine
-
-
-
?
4-nitro-N-benzoyl-L-alanine + H2O
4-nitrobenzoic acid + L-alanine
-
-
-
?
4-nitro-N-benzoylglycine + H2O
4-nitrobenzoic acid + glycine
-
best substrate
-
?
benzyloxycarbonyl-glycyl-L-phenylalanine + H2O
benzoic acid + ?
-
-
-
?
itoic acid + H2O
2,3-dihydroxybenzoic acid + glycine
-
low specificity
-
?
N-(4-nitrobenzoyl)-Gly-Gly-Gly + H2O
4-nitrobenzoic acid + Gly-Gly-Gly
-
-
-
?
N-acetyl-DL-asparagine + H2O
acetic acid + DL-asparagine
-
low activity
-
?
N-acetyl-DL-methionine + H2O
acetic acid + DL-methionine
-
low activity
-
?
N-acetyl-DL-phenylalanine + H2O
acetic acid + DL-phenylalanine
-
low activity
-
?
N-acetyl-DL-valine + H2O
acetic acid + DL-valine
-
very low activity
-
?
N-acetyl-L-glutamine + H2O
acetic acid + L-glutamine
-
low activity
-
?
N-benzoyl-(S-benzoyl)-DL-cysteine + H2O
benzoic acid + S-benzoyl-DL-cysteine
-
low activity
-
?
N-benzoyl-DL-alloisoleucine + H2O
benzoic acid + DL-alloisoleucine
-
-
-
?
N-benzoyl-DL-asparagine + H2O
benzoic acid + DL-asparagine
-
-
-
?
N-benzoyl-DL-phenylalanine + H2O
benzoic acid + DL-phenylalanine
-
-
-
?
N-benzoyl-DL-tryptophan + H2O
benzoic acid + DL-tryptophan
-
low activity
-
?
N-benzoyl-DL-valine + H2O
benzoic acid + DL-valine
-
low activity
-
?
N-benzoyl-L-aminobutyric acid + H2O
benzoic acid + L-aminobutyric acid
-
low activity
-
?
N-benzoyl-L-valine + H2O
benzoic acid + L-valine
-
poor substrate
-
?
N-benzoylglycylglycylglycine + H2O
benzoic acid + glycylglycylglycine
-
-
-
?
additional information
?
-
-
substrate specificity, the enzyme also shows metallocarboxypeptidase activity with carboxypeptidase substrates in vitro, displaying its highest activity against N-benzoyl-linked small aliphatic acids, overview, the enzyme does not hydrolyze typical substrates for aminopeptidases, lysine-p-nitroanilide, leucine-p-nitroanilide, or endopeptidases, N-benzoylarginine-p-nitroanilide, succinylphenylalanine-4-nitroanilide
-
-
?
N-benzoyl-DL-methionine + H2O
benzoic acid + DL-methionine
-
-
-
?
N-benzoyl-DL-methionine + H2O
benzoic acid + DL-methionine
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poor substrate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
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hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
best substrate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
N-benzoylglycine + H2O
benzoic acid + glycine
-
hippurate
-
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
-
1.98 molecules of zinc per enzyme subunit molecule, metalloenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no significant inhibition by E64, PMSF, and pepstatin at 0.5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Campylobacter Infections
The detection of hipO gene by real-time PCR in thermophilic Campylobacter spp. with very weak and negative reaction of hippurate hydrolysis.
Crohn Disease
Molecular detection of Campylobacter jejuni in patients with Crohn's disease in Iran.
Diabetic Foot
Enzymatically active Peptostreptococcus magnus: association with site of infection.
Infections
Enzymatically active Peptostreptococcus magnus: association with site of infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.769
4-aminobenzoyl-glutamate
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pH 7.5, 37°C, purified recombinant wild-type enzyme
5.45
N-acetyl-L-alanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
3.377
N-acetylglycine
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pH 7.5, 37°C, purified recombinant wild-type enzyme
0.169
N-benzoylalanine
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pH 7.5, 37°C, purified recombinant wild-type enzyme
0.159
N-benzoylglutamate
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.303
N-benzoylmethionine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.195
N-benzoylphenylalanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.594
N-benzoylvaline
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14.75
4-aminobenzoyl-glutamate
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
5.95
N-benzoylphenylalanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
2 - 8
N-acetyl-L-alanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
22.12
N-acetyl-L-alanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.052 - 2.1
N-acetylglycine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
10.18
N-acetylglycine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
29.38
N-benzoylalanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
81
N-benzoylalanine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.17
N-benzoylglutamate
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
48.72
N-benzoylglutamate
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
2.6
N-benzoylmethionine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
57.13
N-benzoylmethionine
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
0.5
N-benzoylvaline
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
13.33
N-benzoylvaline
-
pH 7.5, 37°C, purified recombinant wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
induction of enzyme synthesis by hippurate-containing media
brenda
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induction of enzyme synthesis by hippurate-containing media
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (1546 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
the enzyme structure shows highly ordered alpha-helix and beta-sheet sequences
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D76N
-
site-directed mutagenesis, the mutant shows over 12fold reduced activity compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene hipO, expression of His6-tagged enzyme in Escherichia coli strain M15
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
enzymatic determination of Bacillus subtilis siderophore itoic acid and 2,3-dihydroxybenzoic acid
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ito, T.
Enzymic determination of itoic acid, a Bacillus subtilis siderophore, and 2,3-dihydroxybenzoic acid
Appl. Environ. Microbiol.
59
2343-2345
1993
Pseudomonas putida
brenda
Miyagawa, E.; Yano, J.; Hamakado, T.; Kido, Y.; Nishimoto, K.; Motoki, Y.
Crystallization and properties of N-benzoylglycine amidohydrolase from Pseudomonas putida
Agric. Biol. Chem.
49
2881-2886
1985
Pseudomonas putida
-
brenda
Ottow, J.C.G.
Detection of hippurate hydrolase among Bacillus species by thin layer chromatography and other methods
J. Appl. Bacteriol.
37
15-30
1974
Geobacillus stearothermophilus, Paenibacillus alvei, Brevibacillus brevis, Bacillus cereus, Bacillus circulans, Bacillus coagulans, Metabacillus fastidiosus, Cytobacillus firmus, Priestia megaterium, Sporosarcina globispora, Psychrobacillus insolitus, Sporolactobacillus laevolacticus, Brevibacillus laterosporus, Bacillus licheniformis, Paenibacillus macerans, Peribacillus simplex, Bacillus pumilus, Virgibacillus pantothenticus, Sporosarcina pasteurii, Paenibacillus polymyxa, Sporosarcina psychrophila, Paenibacillus larvae subsp. pulvifaciens, Bacillus racemilacticus, Lysinibacillus sphaericus, no activity in Bacillus lentus, no activity in Bacillus macquariensis
brenda
Röhr, M.
Hippurathydrolase, ein neues Enzym aus Mikroorganismen, Darstellung einer gereinigten Enzympräparation und Untersuchungen zur Substratspezifität
Monatsh. Chem.
99
2255-2277
1968
Fusarium incarnatum
-
brenda
Röhr, M.
Hippurathydrolase, ein neues Enzym aus Mikroorganismen, 2. Mitt.: Enzymeigenschaften
Monatsh. Chem.
99
2278-2290
1968
Fusarium incarnatum
-
brenda
Steele, M.; Marcone, M.; Gyles, C.; Chan, V.L.; Odumeru, J.
Enzymatic activity of Campylobacter jejuni hippurate hydrolase
Protein Eng. Des. Sel.
19
17-25
2006
Campylobacter jejuni
brenda
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