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Information on EC 3.4.13.20 - beta-Ala-His dipeptidase and Organism(s) Mus musculus and UniProt Accession Q8BUG2

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.20 beta-Ala-His dipeptidase
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This record set is specific for:
Mus musculus
UNIPROT: Q8BUG2 not found.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carnosinase
-
-
serum carnosinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-21-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carnosine + H2O
beta-Ala + His
show the reaction diagram
-
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
show the reaction diagram
L-carnosine + H2O
beta-Ala + His
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Zn2+ is not required for enzymatic activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
lowers dose-dependently recombinant CN1 efficiency
N-acetylcysteine
lowers dose-dependently recombinant CN1 efficiency
reduced glutathione
lowers dose-dependently recombinant CN1 efficiency
bestatin
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 1.1
carnosine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the enzyme is enriched in several specific neuronal populations in the central nervous system
Manually annotated by BRENDA team
-
highly expressed in tuberomammillary nucleus of the hypothalamus
Manually annotated by BRENDA team
-
highly expressed in the mitral cell layer of the olfactory bulb
Manually annotated by BRENDA team
-
highly expressed in parafascicular nucleus of the thalamus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
reduced glutathione, N-acetylcysteine and cysteine lower dose-dependently recombinant CN1 efficiency and normalize increased CN1 activity in renal tissue samples of diabetic mice. Inhibition is allosteric. Only cysteine-102 is influenced by cysteinylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CNDP1_MOUSE
492
0
55090
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with bestatin together with Zn2+, hanging drop vapour diffusion method, using 20% polyethylene glycol 3350 and 0.2 M potassium fluoride
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C102S
efficiency for carnosine degradation is not influenced by the addition of cysteine
C229S
addition of cysteine to C229S significantly reduces CN1 catalytic efficiency
H228A
-
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose bead chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)pLysS
-
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, K.
X-His dipeptidase
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
1022-1024
2004
Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Otani, H.; Okumura, N.; Hashida-Okumura, A.; Nagai, K.
Identification and characterization of a mouse dipeptidase that hydrolyzes L-carnosine
J. Biochem.
137
167-175
2005
Mus musculus
Manually annotated by BRENDA team
Unno, H.; Yamashita, T.; Ujita, S.; Okumura, N.; Otani, H.; Okumura, A.; Nagai, K.; Kusunoki, M.
Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2
J. Biol. Chem.
283
27289-27299
2008
Mus musculus
Manually annotated by BRENDA team
Min, J.; Senut, M.C.; Rajanikant, K.; Greenberg, E.; Bandagi, R.; Zemke, D.; Mousa, A.; Kassab, M.; Farooq, M.U.; Gupta, R.; Majid, A.
Differential neuroprotective effects of carnosine, anserine, and N-acetyl carnosine against permanent focal ischemia
J. Neurosci. Res.
86
2984-2991
2008
Mus musculus
Manually annotated by BRENDA team
Peters, V.; Schmitt, C.P.; Weigand, T.; Klingbeil, K.; Thiel, C.; van den Berg, A.; Calabrese, V.; Nawroth, P.; Fleming, T.; Forsberg, E.; Wagner, A.H.; Hecker, M.; Vistoli, G.
Allosteric inhibition of carnosinase (CN1) by inducing a conformational shift
J. Enzyme Inhib. Med. Chem.
32
1102-1110
2017
Mus musculus (Q8BUG2)
Manually annotated by BRENDA team