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Information on EC 3.4.13.20 - beta-Ala-His dipeptidase
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EC Tree
3.4.13.20 beta-Ala-His dipeptidaseSpecify your search results
Word Map
- 3.4.13.20
- carnosine
- dipeptide
- nephropathy
- anserine
- homocarnosine
- beta-alanyl-l-histidine
- l-histidine
- bestatin
-
n-acetylcarnosine
-
histidine-containing
-
carcinine
- medicine
- analysis
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
preferential hydrolysis of the beta-Ala-/-His dipeptide (carnosine), and also anserine, Xaa-/-His dipeptides and other dipeptides including homocarnosine
Synonyms
carnosinase, cndp1, serum carnosinase, carnosinase-1, beta-ala-his dipeptidase, cytosolic non-specific dipeptidase 2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carnosinase
CN1
CN2
CNDP1
DmpA
EC 3.4.13.13
-
-
formerly, part transferred
-
EC 3.4.13.3
-
-
formerly, part transferred
-
EC 3.4.3.3
-
-
formerly, part transferred
-
serum carnosinase
serum carnosinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential hydrolysis of the beta-Ala-/-His dipeptide (carnosine), and also anserine, Xaa-/-His dipeptides and other dipeptides including homocarnosine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
9027-21-8
-
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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
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys-beta-homoPhe-beta-homoAla-beta-homoLys-beta-homoPhe
3-(acetylamino)-L-alanyl-L-histidine + H2O
3-(acetylamino)-L-alanine + L-histidine
-
3% of the activity with carnosine
-
-
?
3-amino-L-alanyl-L-histidine + H2O
3-amino-L-alanine + L-histidine
-
30% of the activity with carnosine
-
-
?
beta-Ala-Gly + H2O
beta-Ala + Gly
76% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-L-Leu + H2O
beta-Ala + L-Leu
49% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-NH2 + H2O
beta-Ala + NH3
58% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-homoAla-4-nitroanilide + H2O
beta-homoAla + 4-nitroaniline
-
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
hydrolysis at 55% compared to hydrolysis of carnosine
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
hydrolysis at 0.01% compared to hydrolysis of carnosine
-
-
?
beta-homoPhe-4-nitroanilide + H2O
beta-homoPhe + 4-nitroaniline
-
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
hydrolysis at 0.06% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
hydrolysis at 0.19% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
hydrolysis at 0.01% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-Ile-Tyr + H2O
beta-homoVal + Ile-Tyr
hydrolysis at 0.09% compared to hydrolysis of carnosine
-
-
?
D-Ala-NH2 + H2O
D-Ala + NH3
0.6% of the activity compared to beta-Ala-L-Ala
-
-
?
N-acetyl-3-(acetylamino)-L-alanyl-L-histidine + H2O
N-acetyl-3-(acetylamino)-L-alanine + L-histidine
-
63% of the activity with carnosine
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys-beta-homoPhe-beta-homoAla-beta-homoLys-beta-homoPhe
DmpA cleaves the N-terminal beta-homoAla, no further hydrolysis is observed within 13 days
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys-beta-homoPhe-beta-homoAla-beta-homoLys-beta-homoPhe
Brucella anthropi LMG7991
DmpA cleaves the N-terminal beta-homoAla, no further hydrolysis is observed within 13 days
-
-
?
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
-
88% of the activity with carnosine
-
?
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
-
splitting in the blood stream
-
-
?
beta-Ala-beta-Ala + H2O
beta-Ala + beta-Ala
48% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-beta-Ala + H2O
beta-Ala + beta-Ala
48% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
hydrolysis at 1.3% compared to hydrolysis of carnosine
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
Brucella anthropi LMG7991
hydrolysis at 1.3% compared to hydrolysis of carnosine
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, preferred substrate
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
Brucella anthropi LMG7991
i.e. carnosine, preferred substrate
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 57% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 57% of the activity compared to beta-Ala-L-Ala
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
30% of the activity with Gly-p-nitroanilide, partially purified enzyme
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
Brucella anthropi LMG7991
30% of the activity with Gly-p-nitroanilide, partially purified enzyme
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
16% of the activity compared to beta-Ala-L-Ala. D-Ala-4-nitroanilide is hydrolyzed with 5.8 times high efficiency than L-Ala-4-nitroanilide
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
16% of the activity compared to beta-Ala-L-Ala. D-Ala-4-nitroanilide is hydrolyzed with 5.8 times high efficiency than L-Ala-4-nitroanilide
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
9% of the activity with Gly-p-nitroanilide, partially purified enzyme
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
Brucella anthropi LMG7991
9% of the activity with Gly-p-nitroanilide, partially purified enzyme
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
3% of the activity compared to beta-Ala-L-Ala. D-Ala-4-nitroanilide is hydrolyzed with 5.8 times high efficiency than L-Ala-4-nitroanilide
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
3% of the activity compared to beta-Ala-L-Ala. D-Ala-4-nitroanilide is hydrolyzed with 5.8 times high efficiency than L-Ala-4-nitroanilide
-
-
?
additional information
?
-
cleaves beta- and mixed alpha,beta-peptides and amides, but a short side chain of the N-terminal beta-amino acid residue seems to be a prerequisite, since only peptides carrying N-terminal betahGly and betahAla are hydrolyzed with good efficiencies. Tripeptides carrying two consecutive N-terminal beta-homoamino acids as well as peptides with alpha-amino acids in the N-terminal position do not serve as substrates for DmpA
-
-
?
additional information
?
-
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
the enzyme also shows activity with various dipeptides and tripeptides
-
-
?
additional information
?
-
Brucella anthropi LMG7991
the enzyme also shows activity with various dipeptides and tripeptides
-
-
?
additional information
?
-
Brucella anthropi LMG7991
cleaves beta- and mixed alpha,beta-peptides and amides, but a short side chain of the N-terminal beta-amino acid residue seems to be a prerequisite, since only peptides carrying N-terminal betahGly and betahAla are hydrolyzed with good efficiencies. Tripeptides carrying two consecutive N-terminal beta-homoamino acids as well as peptides with alpha-amino acids in the N-terminal position do not serve as substrates for DmpA
-
-
?
additional information
?
-
Brucella anthropi LMG7991
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
-
no hydrolysis of L-Ala-His, Gly-His or N-acetylhistidine
-
-
?
additional information
?
-
-
dipeptide with histidine in the C-terminal position is preferred
-
-
?
additional information
?
-
-
homocarnosinosis: the lack of serum carnosinase is the defect probably responsible for elevated brain and CSF homocarnosine
-
-
?
additional information
?
-
-
enzyme activities in patients with idiopathic epilepsy and motor neurone disease are similar to the control group. Reduced serum carnosinase activity is observed in patients with multiple sclerosis and patients following a cerebrovascular accident
-
-
?
additional information
?
-
non Xaa-His dipeptides like Ala-Ala, or Ala-Pro, as well as tripeptides containing histidine in central or C-terminal position such as Gly-His-Gly or Gly-Gly-His, are not degraded
-
-
?
additional information
?
-
-
non Xaa-His dipeptides like Ala-Ala, or Ala-Pro, as well as tripeptides containing histidine in central or C-terminal position such as Gly-His-Gly or Gly-Gly-His, are not degraded
-
-
?
additional information
?
-
-
does not hydrolyse beta-Ala-D-His, (3S)-3-amino-4-(phenylbutanoyl)-D-histidine, (3S)-3-(aminobutanoyl)-D-histidine, (3S)-3-amino-4-(4-methoxyphenyl)butanoyl-D-histidine, (3S)-3-amino-3-(3,4-methylenedioxyphenyl)propanoyl-D-histidine, 3-amino-2-(S)-(phenylpropanoyl)-D-histidine, (2R,3S)-3-amino-2-hydroxy-4-(phenylbutanoyl)-D-histidine, (3S)-3-amino-3-(phenylpropanoyl)-D-histidine, (3S)-3-amino-4-(4-hydroxyphenyl)butanoyl-D-histidine, and (3S)-3-amino-3-(4-metoxyphenyl)propanoyl-D-histidine
-
-
?
additional information
?
-
-
S-trolox-L-carnosine (STC) and R-trolox-L-carnosine are resistant toward hydrolytic degradation by human carnosinase
-
-
?
additional information
?
-
no activity on the peptides containing proteinogenic amino acids or their D-counterparts for N-terminal residues. gamma-Aminobutyryl-L-His (L-homocarnosine) is not hydrolyzed
-
-
?
additional information
?
-
no activity on the peptides containing proteinogenic amino acids or their D-counterparts for N-terminal residues. gamma-Aminobutyryl-L-His (L-homocarnosine) is not hydrolyzed
-
-
?
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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
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
-
splitting in the blood stream
-
-
?
additional information
?
-
-
homocarnosinosis: the lack of serum carnosinase is the defect probably responsible for elevated brain and CSF homocarnosine
-
-
?
additional information
?
-
-
enzyme activities in patients with idiopathic epilepsy and motor neurone disease are similar to the control group. Reduced serum carnosinase activity is observed in patients with multiple sclerosis and patients following a cerebrovascular accident
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(acetylamino)-L-alanyl-L-histidine
-
2.3 mM, 50% inhibition of 3-nitrotyrosine formation
3-amino-L-alanyl-L-histidine
-
3.3 mM, 50% inhibition of 3-nitrotyrosine formation
citrate
-
citrate ions are shown to bind at only three well-defined sites involving both ion pairs and hydrogen bonds. Molecular dynamics simulations evidence that citrate binding has a remarkable conformational influence on the 3D structure of carnosinase, increasing the binding affinity of carnosine to the catalytic site
N-acetyl-3-(acetylamino)-L-alanyl-L-histidine
-
2.5 mM, 50% inhibition of 3-nitrotyrosine formation
additional information
-
no inhibition by p-hydroxymercuribenzoate, CH2ClCOONa, phenylmethylsulfonyl fluoride
-
additional information
no inhibition: o-phenanthroline, 8-hydroxyquinoline, ethylenediaminetetraacetic acid, 2,2'-dipyridyl, hydroxylamine, phenylhydrazine, hydrazine, D,L-penicillamine, D-cycloserine, phenylmethanesulfonyl fluoride, leupeptine, pepstatin, LiCl, H2BO3, NaCl, MgSO4, MgCl2, AlCl3, KCl, CaCl2, CrCl3, MnSO4, MnCl2, FeSO4, FeCl3, CoCl2, NiCl2, CuSO4, CuCl2, RbCl, Na2MoO4 (NH4)6Mo7O24, SnCl2, CsCl, BaCl2 and PbCl2
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
Gly-4-nitroanilide
100 mM Tris/HCl or 50 mM potassium phosphate, pH 8.0, 30°C
0.21
carnosine
-
Vmax: 356 pmol/min/microgram after addition of 0.08 mM homocarnosine
0.7
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM glycine
0.8
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM L-glutamate
0.9
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM glutathione
0.9
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM reduced glutathione
1
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM cysteine
1.1
carnosine
pH 7.0, temperature not specified in the publication, presence of 1 mM N-acetylcysteine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70
Gly-4-nitroanilide
100 mM Tris/HCl or 50 mM potassium phosphate, pH 8.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
Gly-4-nitroanilide
100 mM Tris/HCl or 0 mM potassium phosphate, pH 8.0, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE