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Information on EC 3.4.13.5 - Xaa-methyl-His dipeptidase
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3.4.13.5 Xaa-methyl-His dipeptidaseSpecify your search results
Word Map
- 3.4.13.5
-
carnosinase
- dipeptides
- anserine
- homocarnosine
- metallopeptidase
-
oreochromis
-
gadus
- niloticus
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
anserinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylhistidine deacetylase
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aminoacyl-methylhistidine dipeptidase
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anserinase
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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NacHDE
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Nalpha-acetylhistidine deacetylase
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X-methyl-His dipeptidase
Xaa-methyl-His dipeptidase
anserinase
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X-methyl-His dipeptidase
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Xaa-methyl-His dipeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of anserine (beta-alanyl-/-Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl-/-leucine and other dipeptides with broad specificity.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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dipeptide hydrolase
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PATHWAY SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
37289-11-5
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9027-38-7
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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
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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-
?
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
A4F1S8
180% of the activity with L-Ala-L-His
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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-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-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-chloroacetyl-L-Leu + H2O
chloroacetic acid + L-Leu
A4F1S8
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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?
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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83% of the activity with N-acetyl-L-His, brain enzyme
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?
Gly-L-Leu + H2O
Gly + L-Leu
A4F1S8
352% of the activity with L-Ala-L-His
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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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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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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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62% of the activity with carnosine
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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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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
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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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zn2+
additional information
additional information
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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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bestatin
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0.01 mM, 15% inhibition of the enzyme from eye, 1% inhibition of the enzyme from brain
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
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pH 6.0: about 35% of maximal activity, pH 8.0: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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pI VALUE
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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all regions of the brain except for the spinal cord and the optic nerve
brenda
A4F1S8
mRNA is strongly expressed in the liver of Japanese eel
brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
I7GZM3_9HELI
455
0
50477
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, 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
-
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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