We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of anserine (beta-alanyl-/-Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl-/-leucine and other dipeptides with broad specificity.
Synonyms
anserinase, xaa-methyl-his dipeptidase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetylhistidine deacetylase
-
-
-
aminoacyl-methylhistidine dipeptidase
-
-
-
aminoacyl-pros-methyl-L-histidine hydrolase
-
-
deacetylase, acetylhistidine
-
-
-
dipeptidase, aminoacylmethylhistidine
-
-
-
Nalpha-acetylhistidine deacetylase
-
-
-
Xaa-methyl-His dipeptidase
anserinase
-
-
-
ANSN
-
X-methyl-His dipeptidase
-
-
-
X-methyl-His dipeptidase
-
-
Xaa-methyl-His dipeptidase
-
-
-
Xaa-methyl-His dipeptidase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hydrolysis of anserine (beta-alanyl-/-Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl-/-leucine and other dipeptides with broad specificity.
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of peptide bond
-
-
dipeptide hydrolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ala-His + H2O
Ala + His
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
?
anserine + H2O
beta-Ala + 1-methylhistidine
anserine + H2O
beta-alanine + 3-methyl-L-histidine
carnosine + H2O
beta-alanine + L-His
-
-
?
Gly-Gly + H2O
2 Gly
306% of the activity with L-Ala-L-His
-
?
Gly-Gly + H2O
Gly + Gly
-
385% of the activity with N-acetyl-L-His
-
?
Gly-L-His + H2O
Gly + L-His
-
110% of the activity with N-acetyl-L-His, brain enzyme
-
?
Gly-L-Leu + H2O
Gly + L-Leu
Gly-Leu + H2O
Gly + Leu
-
-
-
?
His-Gly + H2O
His + Gly
-
-
?
homocarnosine + H2O
4-aminobutyric acid + L-His
L-Ala-L-His + H2O
L-Ala + L-His
L-Leu-Gly + H2O
L-Leu + Gly
-
101% of the activity with N-acetyl-L-His, brain enzyme
-
?
L-Pro-Gly + H2O
L-Pro + Gly
180% of the activity with L-Ala-L-His
-
?
Leu-Gly + H2O
Leu + Gly
-
-
?
N-acetyl-L-Glu + H2O
L-Glu + acetate
-
23% of the activity with N-acetyl-L-His, brain enzyme
-
?
N-acetyl-L-His + H2O
His + acetate
N-acetyl-L-Leu + H2O
L-Leu + acetate
-
110% of the activity with N-acetyl-L-His, brain enzyme
-
?
N-acetyl-L-methionine + H2O
L-Met + acetate
N-acetyl-L-Trp + H2O
L-Trp + acetate
-
30% of the activity with N-acetyl-L-His, brain enzyme
-
?
Nalpha-acetyl-L-His + H2O
His + acetate
-
-
?
Nalpha-chloro-acetyl-L-Leu + H2O
chloroacetate + Leu
-
-
?
Nalpha-chloroacetyl-L-Leu + H2O
chloroacetic acid + L-Leu
501% of the activity with L-Ala-L-His
-
?
Nalpha-chloroacetyl-L-Leu + H2O
L-Leu + chloroacetate
-
1235% of the activity with N-acetyl-L-His, brain enzyme
-
?
Pro-Gly + H2O
Pro + Gly
-
-
?
additional information
?
-
anserine + H2O
beta-Ala + 1-methylhistidine
-
-
-
?
anserine + H2O
beta-Ala + 1-methylhistidine
-
9% of the activity with carnosine
-
?
anserine + H2O
beta-Ala + 1-methylhistidine
-
16% of the activity with N-acetyl-L-His, brain enzyme
-
?
anserine + H2O
beta-alanine + 3-methyl-L-histidine
-
-
?
anserine + H2O
beta-alanine + 3-methyl-L-histidine
-
-
-
?
carnosine + H2O
?
-
-
-
?
carnosine + H2O
?
-
83% of the activity with N-acetyl-L-His, brain enzyme
-
?
Gly-His + H2O
Gly + His
-
-
-
?
Gly-His + H2O
Gly + His
-
68% of the activity with carnosine
-
?
Gly-L-Leu + H2O
Gly + L-Leu
352% of the activity with L-Ala-L-His
-
?
Gly-L-Leu + H2O
Gly + L-Leu
-
42% of the activity with carnosine
-
?
Gly-L-Leu + H2O
Gly + L-Leu
-
832% of the activity with N-acetyl-L-His, brain enzyme
-
?
homocarnosine + H2O
4-aminobutyric acid + L-His
-
-
?
homocarnosine + H2O
4-aminobutyric acid + L-His
-
-
-
?
homocarnosine + H2O
?
-
102% of the activity with carnosine
-
?
homocarnosine + H2O
?
-
67% of the activity with N-acetyl-L-His, brain enzyme
-
?
L-Ala-L-His + H2O
L-Ala + L-His
-
-
?
L-Ala-L-His + H2O
L-Ala + L-His
-
105% of the activity with N-acetyl-L-His, brain enzyme
-
?
N-acetyl-L-His + H2O
His + acetate
-
-
-
?
N-acetyl-L-His + H2O
His + acetate
-
62% of the activity with carnosine
-
?
N-acetyl-L-His + H2O
His + acetate
-
-
-
?
N-acetyl-L-methionine + H2O
L-Met + acetate
-
-
-
?
N-acetyl-L-methionine + H2O
L-Met + acetate
-
12% of the activity with carnosine
-
?
N-acetyl-L-methionine + H2O
L-Met + acetate
-
254% of the activity with N-acetyl-L-His, brain enzyme
-
?
additional information
?
-
-
no activity with: N-acetylhistamine, N-acetyl-L-Trp, N-acetyl-L-Tyr, N-acetyl-L-Ala, N-acetyl-L-Val, N-acetylglycine, N-acetyl-L-Glu, N-acetyl-L-Asp, N-acetyl-L-Cys, N-acetyl-L-Orn
-
?
additional information
?
-
-
enzyme may be required to degrade N-acetyl-L-histidine after formation of a transient capsular complex
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
-
enzyme may be required to degrade N-acetyl-L-histidine after formation of a transient capsular complex
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
0.1 mM, 20% activation
Zn2+
-
activates
additional information
sequence analysis shows that the enzyme is a member of the M20A metallopeptidase subfamily
additional information
-
sequence analysis shows that the enzyme is a member of the M20A metallopeptidase subfamily
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ag+
-
1 mM, 90% inhibition
bestatin
-
0.01 mM, 15% inhibition of the enzyme from eye, 1% inhibition of the enzyme from brain
Co2+
-
1 mM, 10% inhibition
Cys
-
90% inhibition at 1 mM, 40% inhibition at 0.1 mM
Fe3+
-
1 mM, 94% inhibition
Mn2+
-
1 mM, 30% inhibition
phenylmethylsulfonyl fluoride
-
-
EDTA
-
restored by Zn2+ and Co2+
Hg2+
-
HgCl2
Pb2+
-
1 mM, 80% inhibition
PCMB
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 9
-
less than 10% of maximal activity at pH 5.0 and 9.0
5.2 - 8.5
-
50% of maximal activity at pH 5.2 and at pH 8.5
6 - 8
-
pH 6.0: about 35% of maximal activity, pH 8.0: about 55% of maximal activity
6.5 - 7.8
-
activity is sharply reduced below pH 6.5 and above pH 7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10 - 60
-
10°C: about 50% of maximal activity, brain and eye enzyme, 60°C, about 40% of maximal activity, brain enzyme, 60°C: about 90% of maximal activity, eye enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.3
calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
anserinase precursor
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
trace amounts
brenda
-
moderate activity
brenda
-
brenda
-
cortex, concentrated in the capsule at levels up to 3 mg/ml
brenda
-
-
brenda
-
trace amounts
brenda
-
brenda
-
brenda
-
trace amounts
brenda
-
trace amounts
brenda
-
very rich source
brenda
-
trace amounts
brenda
-
-
brenda
-
very rich source
brenda
-
all regions of the brain except for the spinal cord and the optic nerve
brenda
-
brenda
mRNA is strongly expressed in the liver of Japanese eel
brenda
-
moderate activity
brenda
-
brenda
-
skeletal
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
I7GZM3_9HELI
455
0
50477
TrEMBL
-
A0A377Q3K6_9HELI
433
0
48511
TrEMBL
-
A0A377JW85_9HELI
455
0
50436
TrEMBL
-
A0A3S5BSN5_9HELI
423
0
47551
TrEMBL
-
A0A377JWP2_9HELI
455
0
50454
TrEMBL
-
A0A099TYE4_9HELI
504
0
56519
TrEMBL
-
A0A377J2X7_9HELI
494
0
54275
TrEMBL
-
Q3LHN4_ORENI
494
0
55182
TrEMBL
Secretory Pathway (Reliability: 1 )
A4F1S8_ANGJA
493
0
54745
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A3P6LTL6_9HELI
482
0
52222
TrEMBL
-
A0A3S4YFY9_9HELI
433
0
48512
TrEMBL
-
A0A2X3DGN8_9HELI
513
0
57642
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
450000
dynamic light scattering, both in presence and absence of Mn2+, recombinant protein
52661
x * 52661, calculated
53311
x * 53311, calculated from sequence
55000
-
2 * 55000, SDS-PAGE
120000
-
gel filtration
120000
-
brain and eye enzyme, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer
-
2 * 55000, SDS-PAGE
octamer
8 * 58309, calculated from sequence
?
x * 52661, calculated
?
x * 53311, calculated from sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.7 - 6.4
-
maximal stability at 30°C, pH 4.7-6.4, in presence of ZnSO4
35025
5.2 - 8.1
-
maximal stability
36081
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
-
maximal stability at 30°C, pH 4.7-6.4, in presence of ZnSO4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
partial
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression both in Escherichia coli and HEK 293 cell
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Yamada, S.; Tanaka, Y.; Sameshima, M.; Furuichi, M.
Occurence of Nalpha-acetylhistidine in the muscle and deacetylation by several tissues of nile tilapia (Oreochromis niloticus)
Comp. Biochem. Physiol. B
103
579-583
1992
Oreochromis niloticus
-
brenda
Lenney, J.F.; Baslow, M.H.; Sugiyama, G.H.
Similarity of tuna N-acetylhistidine deacetylase and cod fish anserinase
Comp. Biochem. Physiol. B
61
253-258
1978
Katsuwonus pelamis
brenda
Jones, N.R.
The free amino acids of fish. 1-Methylhistidine and beta-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias)
Biochem. J.
60
81-87
1955
Gadus morhua callarias
brenda
Baslow, M.H.; Lenney, J.F.
Alpha-N-acetyl-L-histidine amidohydrolase activity from the brain of the skipjack tuna Katsuwonus pelamis
Can. J. Biochem.
45
337-349
1967
Katsuwonus pelamis
brenda
Yamada, S.; Tanaka, Y.; Sameshima, M.; Furuichi, M.
Properties of Nalpha-acetylhistidine deacetylase in brain of rainbow trout Oncorhynchus mykiss
Comp. Biochem. Physiol. B
106
309-315
1993
Oncorhynchus mykiss
-
brenda
Yamada, S.; Tanaka, Y.; Ando, S.
Purification and sequence identification of anserinase
FEBS J.
272
6001-6013
2005
Oreochromis niloticus (Q3LHN4), Oreochromis niloticus
brenda
McDonald, J.K.
X-methyl-His dipeptidase
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2
2109-2110
2004
Katsuwonus pelamis
-
brenda
Oku, T.; Ando, S.; Tsai, H.C.; Yamashita, Y.; Ueno, H.; Shiozaki, K.; Nishi, R.; Yamada, S.
Purification and identification of two carnosine-cleaving enzymes, carnosine dipeptidase I and Xaa-methyl-His dipeptidase, from Japanese eel (Anguilla japonica)
Biochimie
94
1281-1290
2012
Anguilla japonica (A4F1S8), Anguilla japonica
brenda
Pirone, L.; Di Gaetano, S.; Rizzarelli, E.; Bellia, F.; Pedone, E.
Focusing on the functional characterization of the anserinase from Oreochromis niloticus
Int. J. Biol. Macromol.
130
158-165
2019
Oreochromis niloticus (Q3LHN4), Oreochromis niloticus
brenda
Select items on the left to see more content.
html completed