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Information on EC 3.4.13.20 - beta-Ala-His dipeptidase and Organism(s) Brucella anthropi and UniProt Accession Q59632

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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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Brucella anthropi
UNIPROT: Q59632 not found.
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The taxonomic range for the selected organisms is: Brucella anthropi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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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
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
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys-beta-homoPhe-beta-homoAla-beta-homoLys-beta-homoPhe
show the reaction diagram
DmpA cleaves the N-terminal beta-homoAla, no further hydrolysis is observed within 13 days
-
-
?
beta-Ala-4-nitroanilide + H2O
beta-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
show the reaction diagram
hydrolysis at 1.3% compared to hydrolysis of carnosine
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
show the reaction diagram
i.e. carnosine, preferred substrate
-
-
?
beta-homoAla-4-nitroanilide + H2O
beta-homoAla + 4-nitroaniline
show the reaction diagram
-
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
show the reaction diagram
hydrolysis at 55% compared to hydrolysis of carnosine
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
show the reaction diagram
hydrolysis at 0.01% compared to hydrolysis of carnosine
-
-
?
beta-homoPhe-4-nitroanilide + H2O
beta-homoPhe + 4-nitroaniline
show the reaction diagram
-
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
show the reaction diagram
hydrolysis at 0.06% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
show the reaction diagram
hydrolysis at 0.19% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
show the reaction diagram
hydrolysis at 0.01% compared to hydrolysis of carnosine
-
-
?
beta-homoVal-Ile-Tyr + H2O
beta-homoVal + Ile-Tyr
show the reaction diagram
hydrolysis at 0.09% compared to hydrolysis of carnosine
-
-
?
D-Ala-4-nitroanilide + H2O
D-Ala + 4-nitroaniline
show the reaction diagram
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0039
beta-Ala-4-nitroanilide
pH 8.0, 25°C
0.019
beta-homoAla-4-nitroanilide
pH 8.0, 25°C
1.1
beta-homoPhe-4-nitroanilide
pH 8.0, 25°C
0.52 - 0.54
D-Ala-4-nitroanilide
3
Gly-4-nitroanilide
100 mM Tris/HCl or 50 mM potassium phosphate, pH 8.0, 30°C
0.36 - 0.6
L-Ala-4-nitroanilide
0.4
L-Arg-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
0.4
L-Lys-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30.5
beta-Ala-4-nitroanilide
pH 8.0, 25°C
51.4
beta-homoAla-4-nitroanilide
pH 8.0, 25°C
0.03
beta-homoPhe-4-nitroanilide
pH 8.0, 25°C
3.3 - 4
D-Ala-4-nitroanilide
70
Gly-4-nitroanilide
100 mM Tris/HCl or 50 mM potassium phosphate, pH 8.0, 30°C
0.5 - 0.56
L-Ala-4-nitroanilide
0.14
L-Arg-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
0.11
L-Lys-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7800
beta-Ala-4-nitroanilide
pH 8.0, 25°C
2600
beta-homoAla-4-nitroanilide
pH 8.0, 25°C
0.027
beta-homoPhe-4-nitroanilide
pH 8.0, 25°C
6.3 - 7.5
D-Ala-4-nitroanilide
23
Gly-4-nitroanilide
100 mM Tris/HCl or 0 mM potassium phosphate, pH 8.0, 30°C
0.8 - 1.55
L-Ala-4-nitroanilide
0.35
L-Arg-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
0.275
L-Lys-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
0.017
L-Phe-4-nitroanilide
50 mM potassium phosphate, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q59632_BRUAN
375
0
40415
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13737
x * 13737 + x * 26564, electrospray mass spectrometry
15000
x * 15000 + x * 30000, SDS-PAGE
26564
x * 13737 + x * 26564, electrospray mass spectrometry
30000
x * 15000 + x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the active protein is derived from the precursor by elimination of the N-terminal Met residue and cleavage of the Gly249-Ser250 peptide bond without additional loss of residues. The active enzyme contains two polypeptides corresponding to residues 2-249 (alpha-subunit) and 250-375 (beta-subunit) of the precursor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
active-site modeling of DmpA. Based on the crystal structure and the catalytic mechanism proposed for DmpA, carnosine is manually introduced into the active site of the enzyme. The model shows that carnosine fits excellently, in line with the high specific activity for this substrate
crystal structure of the enzyme determined to 1.82 A resolution using the multiple isomorphous replacement method. The heterodimer folds into a single domain organised as an alphabetabetaalpha sandwich in which two mixed beta sheets are flanked on both sides by two alpha helices
hangig-drop vapor-diffusion method. Two crystal forms are obtained at 21°C in 13-16% PEG 2000 monomethylether at pH 9.0, adding either 0.2 M magnesium chloride or 1 M lithium chloride. Crystals of the first form belong to the space group C222(1) and diffract to 3.0 A resolution. Crystals of the second form belong to the space group P2(1)2(1)2 and diffract to 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
699-701
1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
Manually annotated by BRENDA team
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
Biochem. J.
341
147-155
1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
Manually annotated by BRENDA team
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
Cell. Mol. Life Sci.
55
812-818
1999
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
Manually annotated by BRENDA team
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
1325-1348
2006
Brucella anthropi (Q59632), Brucella anthropi LMG7991 (Q59632)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team