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(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
-
-
?
Ala-Ala + H2O
Ala + Ala
-
11% of the activity with carnosine
-
-
?
Ala-His + H2O
Ala + His
-
38% of the activity with carnosine
-
-
?
Ala-Leu + H2O
Ala + Leu
-
13% of the activity with carnosine
-
-
?
Ala-Tyr + H2O
Ala + Tyr
-
8% of the activity with carnosine
-
-
?
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
beta-Ala-4-nitroanilide + H2O
beta-Ala + 4-nitroaniline
beta-Ala-Ala + H2O
beta-Ala + Ala
-
10% of the activity with carnosine
-
-
?
beta-Ala-beta-Ala + H2O
beta-Ala + beta-Ala
beta-Ala-Gly + H2O
beta-Ala + Gly
76% of the activity compared to beta-Ala-L-Ala
-
-
?
beta-Ala-His + H2O
beta-Ala + His
-
i.e. carnosine
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
beta-Ala-L-Ala + H2O
beta-Ala + L-Ala
preferred substrate
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
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-Ala-Phe + H2O
beta-Ala + Phe
-
18% of the activity with carnosine
-
-
?
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
-
-
?
carnosine + H2O
beta-Ala + His
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
D-Ala-NH2 + H2O
D-Ala + NH3
0.6% of the activity compared to beta-Ala-L-Ala
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
Gly-Gly + H2O
Gly + Gly
-
7% of the activity with carnosine
-
-
?
Gly-His + H2O
Gly + His
-
37% of the activity with carnosine
-
-
?
Gly-His-Gly + H2O
?
-
13% of the activity with carnosine
-
-
?
Gly-His-Lys + H2O
?
-
7% of the activity with carnosine
-
-
?
Gly-L-His + H2O
Gly + L-His
-
-
-
?
Gly-Leu + H2O
Gly + Leu
-
21% of the activity with carnosine
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
L-Ala-L-His + H2O
L-Ala + L-His
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
L-carnosine + H2O
beta-Ala + His
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
?
Leu-Leu + H2O
Leu + Leu
-
8% of the activity with carnosine
-
-
?
N-acetyl-3-(acetylamino)-L-alanyl-L-histidine + H2O
N-acetyl-3-(acetylamino)-L-alanine + L-histidine
-
63% of the activity with carnosine
-
-
?
N-methylcarnosine + H2O
N-methyl-beta-Ala + L-His
-
-
-
?
Phe-Ala + H2O
Phe + Ala
-
8% of the activity with carnosine
-
-
?
Ser-His + H2O
Ser + His
-
8% of the activity with carnosine
-
-
?
additional information
?
-
(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
DmpA cleaves the N-terminal beta-homoAla, no further hydrolysis is observed within 13 days
-
-
?
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
-
-
-
?
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-4-nitroanilide + H2O
beta-Ala + 4-nitroaniline
-
-
-
?
beta-Ala-4-nitroanilide + H2O
beta-Ala + 4-nitroaniline
-
-
-
?
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
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
i.e. carnosine, preferred substrate
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
i.e. L-carnosine
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
i.e. carnosine
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
i.e. L-carnosine
-
-
?
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
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
-
i.e. L-carnosine
-
-
?
carnosine + H2O
?
-
-
-
-
?
carnosine + H2O
?
-
-
-
?
carnosine + H2O
beta-Ala + His
-
beta-Ala-His
-
-
?
carnosine + H2O
beta-Ala + His
-
beta-Ala-His
-
?
carnosine + H2O
beta-Ala + His
-
splitting in the blood stream
-
?
carnosine + H2O
beta-Ala + His
-
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
-
-
-
?
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
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
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
?
homocarnosine + H2O
?
-
-
-
-
?
homocarnosine + H2O
?
-
-
-
?
homocarnosine + H2O
?
-
11% of the activity with carnosine
-
-
?
homocarnosine + H2O
?
-
splitting of homocarnosine in the brain
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
?
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
-
-
-
?
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
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
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
?
L-carnosine + H2O
beta-Ala + His
-
-
-
?
L-carnosine + H2O
beta-Ala + His
-
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
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
?
-
the enzyme also shows activity with various dipeptides and tripeptides
-
-
?
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
?
-
-
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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Lenney, J.F.; George, R.P.; Weiss, A.M.; Kucera, C.M.; Chan, P.W.H.; Rinzler, G.S.
Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium
Clin. Chim. Acta
123
221-231
1982
Homo sapiens
brenda
Jackson, M.C.; Kucera, C.M.; Lenney, J.F.
Purification and properties of human serum carnosinase
Clin. Chim. Acta
196
193-206
1991
Homo sapiens
brenda
Lenney, J.F.; Peppers, S.C.; Kucera, C.M.; Ottar, S.
Homocarnosinosis: lack of serum carnosinase is the defect probably responsible for elevated brain and CSF homocarnosine
Clin. Chim. Acta
132
157-165
1983
Homo sapiens
brenda
Schoen, P.; Everts, H.; de Boer, T.; van Oeveren, W.
Serum carnosinase activity in plasma and serum: validation of a method and values in cardiopulmonary bypass surgery
Clin. Chem.
49
1930-1932
2003
Homo sapiens
brenda
Wassif, W.S.; Sherwood, R.A.; Amir, A.; Idowu, B.; Summers, B.; Leigh, N.; Peters, T.J.
Serum carnosinase activities in central nervous system disorders
Clin. Chim. Acta
225
57-64
1994
Homo sapiens
brenda
Cacciatore, I.; Cocco, A.; Costa, M.; Fontana, M.; Lucente, G.; Pecci, L.; Pinnen, F.
Biochemical properties of new synthetic carnosine analogues containing the residue of 2,3-diaminopropionic acid: the effect of N-acetylation
Amino Acids
28
77-83
2005
Homo sapiens
brenda
Zhang, H.; Chen, J.; Waldherr, C.; Hinni, K.; Waser, B.; Reubi, J.C.; Maecke, H.R.
Synthesis and evaluation of bombesin derivatives on the basis of pan-bombesin peptides labeled with indium-111, lutetium-177, and yttrium-90 for targeting bombesin receptor-expressing tumors
Cancer Res.
64
6707-6715
2004
Homo sapiens
brenda
Janssen, B.; Hohenadel, D.; Brinkkoetter, P.; Peters, V.; Rind, N.; Fischer, C.; Rychlik, I.; Cerna, M.; Romzova, M.; de Heer, E.; Baelde, H.; Bakker, S.J.; Zirie, M.; Rondeau, E.; Mathieson, P.; Saleem, M.A.; Meyer, J.; Koeppel, H.; Sauerhoefer, S.; Bartram, C.R.; Nawroth, P.; Hammes, H.P.; Yard, B.A.; Zschocke, J.; van der Woude, F.J.
Carnosine as a protective factor in diabetic nephropathy: association with a leucine repeat of the carnosinase gene CNDP1
Diabetes
54
2320-2327
2005
Homo sapiens
brenda
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
-
brenda
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
brenda
Vistoli, G.; Pedretti, A.; Cattaneo, M.; Aldini, G.; Testa, B.
Homology modeling of human serum carnosinase, a potential medicinal target, and MD simulations of its allosteric activation by citrate
J. Med. Chem.
49
3269-3277
2006
Homo sapiens
brenda
Balion, C.M.; Benson, C.; Raina, P.S.; Papaioannou, A.; Patterson, C.; Ismaila, A.S.
Brain type carnosinase in dementia: a pilot study
BMC Neurol.
7
38
2007
Homo sapiens
brenda
Riedl, E.; Koeppel, H.; Brinkkoetter, P.; Sternik, P.; Steinbeisser, H.; Sauerhoefer, S.; Janssen, B.; van der Woude, F.J.; Yard, B.A.
A CTG polymorphism in the CNDP1 gene determines the secretion of serum carnosinase in Cos-7 transfected cells
Diabetes
56
2410-2413
2007
Homo sapiens
brenda
Sauerhoefer, S.; Yuan, G.; Braun, G.S.; Deinzer, M.; Neumaier, M.; Gretz, N.; Floege, J.; Kriz, W.; van der Woude, F.; Moeller, M.J.
L-carnosine, a substrate of carnosinase-1, influences glucose metabolism
Diabetes
56
2425-2432
2007
Homo sapiens
brenda
Teufel, M.; Saudek, V.; Ledig, J.P.; Bernhardt, A.; Boularand, S.; Carreau, A.; Cairns, N.J.; Carter, C.; Cowley, D.J.; Duverger, D.; Ganzhorn, A.J.; Guenet, C.; Heintzelmann, B.; Laucher, V.; Sauvage, C.; Smirnova, T.
Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase
J. Biol. Chem.
278
6521-31
2002
Homo sapiens (Q96KN2), Homo sapiens
brenda
Kurata, H.; Fujii, T.; Tsutsui, H.; Katayama, T.; Ohkita, M.; Takaoka, M.; Tsuruoka, N.; Kiso, Y.; Ohno, Y.; Fujisawa, Y.; Shokoji, T.; Nishiyama, A.; Abe, Y.; Matsumura, Y.
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Rattus norvegicus
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Zschocke, J.; Nebel, A.; Wicks, K.; Peters, V.; El Mokhtari, N.E.; Krawczak, M.; van der Woude, F.; Janssen, B.; Schreiber, S.
llelic variation in the CNDP1 gene and its lack of association with longevity and coronary heart disease
Mech. Ageing Dev.
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2006
Homo sapiens
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Otani, H.; Okumura, A.; Nagai, K.; Okumura, N.
Colocalization of a carnosine-splitting enzyme, tissue carnosinase (CN2)/cytosolic non-specific dipeptidase 2 (CNDP2), with histidine decarboxylase in the tuberomammillary nucleus of the hypothalamus
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2008
Rattus norvegicus
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Vistoli, G.; Orioli, M.; Pedretti, A.; Regazzoni, L.; Canevotti, R.; Negrisoli, G.; Carini, M.; Aldini, G.
Design, synthesis, and evaluation of carnosine derivatives as selective and efficient sequestering agents of cytotoxic reactive carbonyl species
ChemMedChem
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2009
Homo sapiens
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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
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Mus musculus
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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
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Mus musculus
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Araujo, E.C.; Suen, V.M.; Marchini, J.S.; Vannucchi, H.
Muscle mass gain observed in patients with short bowel syndrome subjected to resistance training
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Homo sapiens
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Bompard-Gilles, C.; Villeret, V.; Fanuel, L.; Joris, B.; Frre, J.M.; Van Beeumen, J.
Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis
Acta Crystallogr. Sect. D
55
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1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
brenda
Peters, V.; Kebbewar, M.; Jansen, E.W.; Jakobs, C.; Riedl, E.; Koeppel, H.; Frey, D.; Adelmann, K.; Klingbeil, K.; Mack, M.; Hoffmann, G.F.; Janssen, B.; Zschocke, J.; Yard, B.A.
Relevance of allosteric conformations and homocarnosine concentration on carnosinase activity
Amino Acids
38
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2010
Homo sapiens
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Yeum, K.J.; Orioli, M.; Regazzoni, L.; Carini, M.; Rasmussen, H.; Russell, R.M.; Aldini, G.
Profiling histidine dipeptides in plasma and urine after ingesting beef, chicken or chicken broth in humans
Amino Acids
38
847-858
2010
Homo sapiens (Q96KN2), Homo sapiens
brenda
Bellia, F.; Calabrese, V.; Guarino, F.; Cavallaro, M.; Cornelius, C.; De Pinto, V.; Rizzarelli, E.
Carnosinase levels in aging brain: redox state induction and cellular stress response
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2009
Homo sapiens
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Inaba, C.; Higuchi, S.; Morisaka, H.; Kuroda, K.; Ueda, M.
Synthesis of functional dipeptide carnosine from nonprotected amino acids using carnosinase-displaying yeast cells
Appl. Microbiol. Biotechnol.
86
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2010
Homo sapiens (Q96KN2)
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Fanuel, L.; Goffin, C.; Cheggour, A.; Devreese, B.; Van Driessche, G.; Joris, B.; Van, Beeumen, J.; Frre, J.M.
The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family
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1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
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Fanuel, L.; Thamm, I.; Kostanjevecki, V.; Samyn, B.; Joris, B.; Goffin, C.; Brannigan, J.; van Beeumen, J.; Frre, J.M.
Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide
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55
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1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
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Stvolinsky, S.L.; Bulygina, E.R.; Fedorova, T.N.; Meguro, K.; Sato, T.; Tyulina, O.V.; Abe, H.; Boldyrev, A.A.
Biological activity of novel synthetic derivatives of carnosine
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2010
Homo sapiens
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Heck, T.; Limbach, M.; Geueke, B.; Zacharias, M.; Gardiner, J.; Kohler, H.P.; Seebach, D.
Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides
Chem. Biodivers.
3
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2006
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
brenda
Heck, T.; Kohler, H.P.; Limbach, M.; Flgel, O.; Seebach, D.; Geueke, B.
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
brenda
Komeda, H.; Asano, Y.
A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for beta-alanyl dipeptides
FEBS J.
272
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2005
Pseudomonas sp. (Q4R9M3), Pseudomonas sp. MCI3434 (Q4R9M3)
brenda
Bompard-Gilles, C.; Villeret, V.; Davies, G.J.; Fanuel, L.; Joris, B.; Frre, J.M.; Van Beeumen, J.
A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi
Structure
8
153-162
2000
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
brenda
Zhang, S.; Albrecht, T.; Rodriguez-Nino, A.; Qiu, J.; Schnuelle, P.; Peters, V.; Schmitt, C.P.; van den Born, J.; Bakker, S.J.L.; Lammert, A.; Kraemer, B.K.; Yard, B.A.; Hauske, S.J.
Carnosinase concentration, activity, and CNDP1 genotype in patients with type 2 diabetes with and without nephropathy
Amino Acids
51
611-617
2019
Homo sapiens (Q96KN2), Homo sapiens
brenda
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)
brenda
Zhang, S.; Lindner, H.; Kabtni, S.; Van Den Born, J.; Bakker, S.; Navis, G.; Kraemer, B.; Yard, B.; Hauske, S.
Monoclonal antibody RYSK173 recognizes the dinuclear Zn center of serum carnosinase 1 (CN-1) Possible consequences of Zn binding for CN-1 recognition by RYSK173
PLoS ONE
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e0146831
2016
Homo sapiens (Q96KN2), Homo sapiens
brenda