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Information on EC 3.4.13.20 - beta-Ala-His dipeptidase and Organism(s) Homo sapiens and UniProt Accession Q96KN2
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3.4.13.20 beta-Ala-His dipeptidaseSpecify your search results
Word Map
- 3.4.13.20
- carnosine
- dipeptide
- nephropathy
- anserine
- homocarnosine
- beta-alanyl-l-histidine
- l-histidine
- bestatin
-
n-acetylcarnosine
-
histidine-containing
-
carcinine
- medicine
- analysis
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
serum carnosinase
serum carnosinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY
9027-21-8
-
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
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
-
-
?
N-acetyl-3-(acetylamino)-L-alanyl-L-histidine + H2O
N-acetyl-3-(acetylamino)-L-alanine + L-histidine
-
63% of the activity with carnosine
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
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
anserine + H2O
beta-Ala + Ntau-methyl-L-histidine
-
splitting in the blood stream
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-(acetylamino)-L-alanyl-L-histidine
-
2.3 mM, 50% inhibition of 3-nitrotyrosine formation
3-amino-L-alanyl-L-histidine
-
3.3 mM, 50% inhibition of 3-nitrotyrosine formation
citrate
-
citrate ions are shown to bind at only three well-defined sites involving both ion pairs and hydrogen bonds. Molecular dynamics simulations evidence that citrate binding has a remarkable conformational influence on the 3D structure of carnosinase, increasing the binding affinity of carnosine to the catalytic site
N-acetyl-3-(acetylamino)-L-alanyl-L-histidine
-
2.5 mM, 50% inhibition of 3-nitrotyrosine formation
additional information
-
no inhibition by p-hydroxymercuribenzoate, CH2ClCOONa, phenylmethylsulfonyl fluoride
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.21
carnosine
-
Vmax: 356 pmol/min/microgram after addition of 0.08 mM homocarnosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CN1 activity is considerably higher in serum than in cerebrospinal fluid
additional information
-
the enzyme activity in tissues is roughly proportional to blood content for all the tissues except brain, indicating that serum carnosinase is present in the trapped blood of these tissues
-
substantial decrease in serum carnosinase activity at the onset and during cardiopulmonary bypass surgery. Just before anesthesia, heparinization, opening of the thoracic cavity, and administration of any additional drugs, the mean serum carnosinase activity decreases by 35%
-
the enzyme is synthesized in brain, where it is secreted into cerebrospinal fluid
-
CN1 activity is considerably higher in serum than in cerebrospinal fluid
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
carnosine and anserine are mainly hydrolyzed by carnosinase, a low but significant amount is excreted in the urine. Carnosine reaches a steady state of very low concentration in serum, while anserine sustains higher concentrations than that of carnosine due to its greater stability vis-a-vis carnosinase after ingesting histidine-dipeptide rich diet
malfunction
-
HeLa-CN1 cells have a lower cell survival than do non-transfected cells or HeLa cells transfected with an empty or a mock vector. Viability in HeLa cells measured after H2O2 treatment is significantly higher than the viability of HeLa-CN1 cells after the same oxidant insult, indicating an increased susceptibility to oxidative stress of cells overexpressing carnosinase
physiological function
-
CN1 activity is lower in children and increases with age with no differences in protein concentration. CN1 activity is considerably higher in serum than in cerebrospinal fluid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CNDP1_HUMAN
507
0
56692
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75000
-
2 * 75000, subunits are connected by one or more disulfide bonds, SDS-PAGE
86000
-
x* 92000, SDS-PAGE of secreted protein, x * 86000 and x * 88000, SDS-PAGE of cytosolic protein
88000
-
x* 92000, SDS-PAGE of secreted protein, x * 86000 and x * 88000, SDS-PAGE of cytosolic protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x* 92000, SDS-PAGE of secreted protein, x * 86000 and x * 88000, SDS-PAGE of cytosolic protein
dimer
-
2 * 75000, subunits are connected by one or more disulfide bonds, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
after treatment with PNGase F, molecular mass shifts from 82000 Da to 62000 Da, SDS-PAGE
glycoprotein
glycoprotein
-
secreted enzyme shows a molecular weight of 92000 Da, cytosolic protein of 86000 Da and 88000 Da, respectively. PNGase-treated protein has a molecular weight of 86000 Da
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E201A/D229A
mutation in putative metal binding site, complete loss of activity
additional information
additional information
using human CN1 gene a whole cell biocatalyst displaying CN1 on the yeast cell surface with alpha-agglutinin as the anchor protein is constructed. CN1-displaying yeast cells show hydrolytic activity for carnosine in hydrophobic organic solvents. CN1-displaying yeast cells can synthesize carnosine from nonprotected amino acids as substrates in hydrophobic organic solvents and in a hydrophobic ionic liquid
additional information
-
expression of constructs varying in CTG repeats coding for 4,5,6,7,or 8 leucines in the signal peptide. Enzyme secretion is significantly higher in cells expressing variants with more than five leucins in the signal peptide
additional information
-
liver-specific expression of enzyme in db/db mice, a model of type 2 diabetes. Transgenic mice shows reduced body weight as a result of glucosuria. Fasting plasma glucose as well as hemoglobin A1C levels rise earlier and remain higher throughout their life than in control animals. Serum fasting insulin levels are low and elevated by L-carnosine feeding. Insulin resistance and insulin secretion are not significantly affected by L-carnosine serum levels. Instead, a significant correlation of L-carnosine levels with beta-cell mass is observed
additional information
-
natural polymorphisms of CDNP12 gene. Detection of a rare 8-leucine allele, of a rare duplication, p.L13_V15dup, and a frameshift deletion, L17fsX20
additional information
-
transfection of Cos-7 cells with different gene constructs varying in CTG repeats. CNDP1 secretion is significantly higher in cells expressing variants with more than five leucines in the signal peptide of the protein. With increasing length of the CTG repeat, the percentage of secreted carnosinase increases
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
up to 8 h the activity remains within 97.5% of the initial value, thereafter the activity decreases slowly
50
-
30 min, pH 7.8, stable, thermostability improved by the presence of 0.25 mM MnCl2, stability is very poor in the presence of 0.25 mM cadmium or calcium
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation during DEAE-cellulose chromatography, slow reactivation when concentrated and stored at 4°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
human CN1 gene is expressed in Saccharomyces cerevisiae on the yeast cell surface with alpha-agglutinin as the anchor protein
a stable HeLa cell line expressing recombinant human serum carnosinase CN1 is established
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
analysis
-
a validated method for measuring serum carnosinase activity in serum and heparin plasma
medicine
medicine
monoclonal antibody RYSK173 recognizes a sequence within the transition metal binding site of CNDP1. The CN-1 RYSK173 proportion appears overall increased in end-stage renal disease patients, yet it decreases during hemodialysis possibly as a consequence of a relative increase in transition metal bound enzyme
medicine
serum CNDP1 concentrations associate with CNDP1 genotype and renal function in patients with type 2 diabetes mellitus. CNDP1 (CTG)5 homozygous patients with type 2 diabetes mellitus with diabetic nephropathy have significantly lower CNDP1 concentrations and activity than those without nephropathy. Lower serum CNDP1 concentrations correlate with impaired renal function and to a lesser extend with the CNDP1 genotype
medicine
-
diabetic patients with the CDDP1 Mannheim variant(shortest allelic form) are less susceptible for nephropathy
medicine
-
CNDP1 secretion is significantly higher in cells expressing variants with more than five leucines in the signal peptide of the protein. This explains why individuals homozygous for the 5L allele have low serum carnosinase activity and why diabetic patients homozygous for CNDP1 5L are protected against diabetic nephropathy
medicine
-
liver-specific expression of enzyme in db/db mice, a model of type 2 diabetes. Transgenic mice shows reduced body weight as a result of glucosuria. Fasting plasma glucose as well as hemoglobin A1C levels rise earlier and remain higher throughout their life than in control animals. Serum fasting insulin levels are low and elevated by L-carnosine feeding. Insulin resistance and insulin secretion are not significantly affected by L-carnosine serum levels. Instead, a significant correlation of L-carnosine levels with beta-cell mass is observed
medicine
-
no difference in allele or genotype frequency between centenarians and their control group, or between vascular patiens and their control group. Detection of a rare 8-leucine allele, of a rare duplication, p.L13_V15dup, and a frameshift deletion, L17fsX20
medicine
-
study on carnosinase activity in patients with Alzheimer's disease and with mixed dementia. Enzyme activity levels in the mixed disease group are significantly lower than the Alzheimer's disease group and the mixed disease group demonstrates a significant trend with carnosidase activity decreasing with duration of disease. Both Alzheimer and mixed disease patients on any demetia medication have higher carnosinase activity compared to those not taking a dementia medication, and enzyme activity is higher in patients who regurlarly exercise compared to those who do not exercise regurlarly
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
-
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
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
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
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
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
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.
127
817-820
2006
Homo sapiens
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
4
967-975
2009
Homo sapiens
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
Nutr. Res.
28
78-82
2008
Homo sapiens
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
1607-1615
2010
Homo sapiens
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
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
Antioxid. Redox Signal.
11
2759-2775
2009
Homo sapiens
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
1895-1902
2010
Homo sapiens (Q96KN2)
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
Cell. Mol. Neurobiol.
30
395-404
2010
Homo sapiens
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
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
11
e0146831
2016
Homo sapiens (Q96KN2), Homo sapiens
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