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Information on EC 3.4.13.5 - Xaa-methyl-His dipeptidase for references in articles please use BRENDA:EC3.4.13.5
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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of anserine (beta-alanyl-/-Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl-/-leucine and other dipeptides with broad specificity.
Synonyms
acetylhistidine deacetylase, aminoacyl-methylhistidine dipeptidase, aminoacyl-pros-methyl-L-histidine hydrolase, anserinase, ANSN, deacetylase, acetylhistidine, dipeptidase, aminoacylmethylhistidine, EC 3.4.3.4, EC 3.5.1.34, NacHDE,
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acetylhistidine deacetylase
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aminoacyl-methylhistidine dipeptidase
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aminoacyl-pros-methyl-L-histidine hydrolase
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deacetylase, acetylhistidine
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dipeptidase, aminoacylmethylhistidine
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EC 3.4.3.4
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formerly
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EC 3.5.1.34
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formerly
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Nalpha-acetylhistidine deacetylase
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Xaa-methyl-His dipeptidase
anserinase
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X-methyl-His dipeptidase
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X-methyl-His dipeptidase
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Xaa-methyl-His dipeptidase
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Xaa-methyl-His dipeptidase
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Hydrolysis of anserine (beta-alanyl-/-Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl-/-leucine and other dipeptides with broad specificity.
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hydrolysis of peptide bond
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dipeptide hydrolase
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Ala-His + H2O
Ala + His
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-
-
?
Ala-Pro + H2O
Ala + Pro
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-
-
?
anserine + H2O
beta-Ala + 1-methylhistidine
anserine + H2O
beta-alanine + 3-methyl-L-histidine
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-
-
?
carnosine + H2O
beta-alanine + L-His
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-
-
?
Gly-Gly + H2O
2 Gly
306% of the activity with L-Ala-L-His
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-
?
Gly-Gly + H2O
Gly
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-
-
?
Gly-Gly + H2O
Gly + Gly
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385% of the activity with N-acetyl-L-His
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-
?
Gly-L-His + H2O
Gly + L-His
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110% of the activity with N-acetyl-L-His, brain enzyme
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-
?
Gly-L-Leu + H2O
Gly + L-Leu
Gly-Leu + H2O
Gly + Leu
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-
-
-
?
His-Gly + H2O
His + Gly
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-
-
?
homocarnosine + H2O
4-aminobutyric acid + L-His
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-
-
?
L-Ala-L-His + H2O
L-Ala + L-His
L-Leu-Gly + H2O
L-Leu + Gly
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101% of the activity with N-acetyl-L-His, brain enzyme
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-
?
L-Pro-Gly + H2O
L-Pro + Gly
180% of the activity with L-Ala-L-His
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?
Leu-Gly + H2O
Leu + Gly
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-
-
?
N-acetyl-L-Glu + H2O
L-Glu + acetate
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23% of the activity with N-acetyl-L-His, brain enzyme
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-
?
N-acetyl-L-His + H2O
His + acetate
N-acetyl-L-Leu + H2O
L-Leu + acetate
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110% of the activity with N-acetyl-L-His, brain enzyme
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-
?
N-acetyl-L-methionine + H2O
L-Met + acetate
N-acetyl-L-Trp + H2O
L-Trp + acetate
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30% of the activity with N-acetyl-L-His, brain enzyme
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-
?
Nalpha-acetyl-L-His + H2O
His + acetate
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?
Nalpha-chloro-acetyl-L-Leu + H2O
chloroacetate + Leu
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-
?
Nalpha-chloroacetyl-L-Leu + H2O
chloroacetic acid + L-Leu
501% of the activity with L-Ala-L-His
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-
?
Nalpha-chloroacetyl-L-Leu + H2O
L-Leu + chloroacetate
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1235% of the activity with N-acetyl-L-His, brain enzyme
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-
?
Pro-Gly + H2O
Pro + Gly
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?
additional information
?
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anserine + H2O
beta-Ala + 1-methylhistidine
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?
anserine + H2O
beta-Ala + 1-methylhistidine
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9% of the activity with carnosine
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?
anserine + H2O
beta-Ala + 1-methylhistidine
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16% of the activity with N-acetyl-L-His, brain enzyme
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?
carnosine + H2O
?
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-
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?
carnosine + H2O
?
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83% of the activity with N-acetyl-L-His, brain enzyme
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?
Gly-His + H2O
Gly + His
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?
Gly-His + H2O
Gly + His
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68% of the activity with carnosine
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?
Gly-L-Leu + H2O
Gly + L-Leu
352% of the activity with L-Ala-L-His
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?
Gly-L-Leu + H2O
Gly + L-Leu
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42% of the activity with carnosine
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Gly-L-Leu + H2O
Gly + L-Leu
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832% of the activity with N-acetyl-L-His, brain enzyme
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?
homocarnosine + H2O
?
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102% of the activity with carnosine
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?
homocarnosine + H2O
?
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67% of the activity with N-acetyl-L-His, brain enzyme
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-
?
L-Ala-L-His + H2O
L-Ala + L-His
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?
L-Ala-L-His + H2O
L-Ala + L-His
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105% of the activity with N-acetyl-L-His, brain enzyme
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?
N-acetyl-L-His + H2O
His + acetate
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?
N-acetyl-L-His + H2O
His + acetate
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62% of the activity with carnosine
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?
N-acetyl-L-His + H2O
His + acetate
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?
N-acetyl-L-methionine + H2O
L-Met + acetate
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?
N-acetyl-L-methionine + H2O
L-Met + acetate
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12% of the activity with carnosine
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?
N-acetyl-L-methionine + H2O
L-Met + acetate
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254% of the activity with N-acetyl-L-His, brain enzyme
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?
additional information
?
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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
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additional information
?
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enzyme may be required to degrade N-acetyl-L-histidine after formation of a transient capsular complex
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additional information
?
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enzyme may be required to degrade N-acetyl-L-histidine after formation of a transient capsular complex
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additional information
sequence analysis shows that the enzyme is a member of the M20A metallopeptidase subfamily
Co2+
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0.1 mM, 20% activation
Zn2+
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activates
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Ag+
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1 mM, 90% inhibition
bestatin
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0.01 mM, 15% inhibition of the enzyme from eye, 1% inhibition of the enzyme from brain
Co2+
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1 mM, 10% inhibition
Cys
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90% inhibition at 1 mM, 40% inhibition at 0.1 mM
Fe3+
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1 mM, 94% inhibition
Mn2+
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1 mM, 30% inhibition
phenylmethylsulfonyl fluoride
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EDTA
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restored by Zn2+ and Co2+
Hg2+
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HgCl2
Pb2+
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1 mM, 80% inhibition
PCMB
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additional information
additional information
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5 - 9
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less than 10% of maximal activity at pH 5.0 and 9.0
5.2 - 8.5
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50% of maximal activity at pH 5.2 and at pH 8.5
6 - 8
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pH 6.0: about 35% of maximal activity, pH 8.0: about 55% of maximal activity
6.5 - 7.8
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activity is sharply reduced below pH 6.5 and above pH 7.8
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10 - 60
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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
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5.3
calculated from sequence
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
anserinase precursor
SwissProt
brenda
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brenda
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trace amounts
brenda
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moderate activity
brenda
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brenda
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cortex, concentrated in the capsule at levels up to 3 mg/ml
brenda
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brenda
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trace amounts
brenda
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brenda
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brenda
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trace amounts
brenda
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trace amounts
brenda
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very rich source
brenda
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trace amounts
brenda
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very rich source
brenda
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brenda
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all regions of the brain except for the spinal cord and the optic nerve
brenda
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brenda
mRNA is strongly expressed in the liver of Japanese eel
brenda
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moderate activity
brenda
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brenda
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skeletal
brenda
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brenda
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A0A377JWP2_9HELI
455
0
50454
TrEMBL
A0A3S5BSN5_9HELI
423
0
47551
TrEMBL
Q3LHN4_ORENI
494
0
55182
TrEMBL
I7GZM3_9HELI
455
0
50477
TrEMBL
A0A3S4YFY9_9HELI
433
0
48512
TrEMBL
A0A3P6LTL6_9HELI
482
0
52222
TrEMBL
A0A377J2X7_9HELI
494
0
54275
TrEMBL
A0A377Q3K6_9HELI
433
0
48511
TrEMBL
A4F1S8_ANGJA
493
0
54745
TrEMBL
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52661
x * 52661, calculated
53311
x * 53311, calculated from sequence
55000
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2 * 55000, SDS-PAGE
120000
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brain and eye enzyme, gel filtration
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dimer
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2 * 55000, SDS-PAGE
?
x * 52661, calculated
?
x * 53311, calculated from sequence
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4.7 - 6.4
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maximal stability at 30°C, pH 4.7-6.4, in presence of ZnSO4
35025
5.2 - 8.1
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maximal stability
36081
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30
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maximal stability at 30°C, pH 4.7-6.4, in presence of ZnSO4
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partial
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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
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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
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brenda
Yamada, S.; Tanaka, Y.; Ando, S.
Purification and sequence identification of anserinase
FEBS J.
272
6001-6013
2005
Oreochromis niloticus, Oreochromis niloticus (Q3LHN4)
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
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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
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3.4.13.5 Xaa-methyl-His dipeptidase
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