3.4.13.20: beta-Ala-His dipeptidase
This is an abbreviated version!
For detailed information about beta-Ala-His dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.20
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3.4.13.20
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carnosine
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dipeptide
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nephropathy
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anserine
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homocarnosine
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beta-alanyl-l-histidine
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l-histidine
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bestatin
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n-acetylcarnosine
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histidine-containing
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carcinine
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medicine
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analysis
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synthesis
- 3.4.13.20
- carnosine
- dipeptide
- nephropathy
- anserine
- homocarnosine
- beta-alanyl-l-histidine
- l-histidine
- bestatin
-
n-acetylcarnosine
-
histidine-containing
-
carcinine
- medicine
- analysis
- synthesis
Reaction
preferential hydrolysis of the beta-Ala-/-His dipeptide (carnosine), and also anserine, Xaa-/-His dipeptides and other dipeptides including homocarnosine =
Synonyms
carnosinase, carnosinase-1, CN1, CN2, CNDP dipeptidase 2, CNDP1, CNDP2, cytosolic non-specific dipeptidase 2, DmpA, EC 3.4.13.13, EC 3.4.13.3, EC 3.4.3.3, serum carnosinase, tissue carnosinase
ECTree
3.4.13.20 beta-Ala-His dipeptidaseAdvanced search results
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Engineering on EC 3.4.13.20 - beta-Ala-His dipeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G249A
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
G249D
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
S250A
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
S250C
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
S250T
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
G249A
Brucella anthropi LMG7991
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the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
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G249D
Brucella anthropi LMG7991
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the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
-
S250A
Brucella anthropi LMG7991
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the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
-
S250C
Brucella anthropi LMG7991
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the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
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S250T
Brucella anthropi LMG7991
-
the precursor is not processeed at the Gly249-Ser250 peptide bond. Production of an uncleaved and inactive protein
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E201A/D229A
mutation in putative metal binding site, complete loss of activity
C102S
efficiency for carnosine degradation is not influenced by the addition of cysteine
C229S
addition of cysteine to C229S significantly reduces CN1 catalytic efficiency
additional information
additional information
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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
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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
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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
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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
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
