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Literature summary extracted from

  • Komeda, H.; Asano, Y.
    A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for beta-alanyl dipeptides (2005), FEBS J., 272, 3075-3084.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.20 expression in Escherichia coli Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.13.20 AgNO3 30°C, 10 min, 1 mM, 95% loss of activity Pseudomonas sp.
3.4.13.20 CdCl2 30°C, 10 min, 1 mM, 90% loss of activity Pseudomonas sp.
3.4.13.20 dithiothreitol 30°C, 10 min, 1 mM, 63% loss of activity Pseudomonas sp.
3.4.13.20 HgCl2 30°C, 10 min, 1 mM, 99% loss of activity Pseudomonas sp.
3.4.13.20 additional information no inhibition: o-phenanthroline, 8-hydroxyquinoline, ethylenediaminetetraacetic acid, 2,2'-dipyridyl, hydroxylamine, phenylhydrazine, hydrazine, D,L-penicillamine, D-cycloserine, phenylmethanesulfonyl fluoride, leupeptine, pepstatin, LiCl, H2BO3, NaCl, MgSO4, MgCl2, AlCl3, KCl, CaCl2, CrCl3, MnSO4, MnCl2, FeSO4, FeCl3, CoCl2, NiCl2, CuSO4, CuCl2, RbCl, Na2MoO4 (NH4)6Mo7O24, SnCl2, CsCl, BaCl2 and PbCl2 Pseudomonas sp.
3.4.13.20 N-ethylmaleimide 30°C, 10 min, 1 mM, 80% loss of activity Pseudomonas sp.
3.4.13.20 p-chloromercuribenzoate 30°C, 10 min, 1 mM, 95% loss of activity Pseudomonas sp.
3.4.13.20 ZnCl2 30°C, 10 min, 1 mM, 98% loss of activity Pseudomonas sp.
3.4.13.20 ZnSO4 30°C, 10 min, 1 mM, 98% loss of activity Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.13.20 13000
-
 alpha4beta4, 2 * 13000 + 2 * 27000, SDS-PAGE Pseudomonas sp.
3.4.13.20 27000
-
 alpha4beta4, 2 * 13000 + 2 * 27000, SDS-PAGE Pseudomonas sp.
3.4.13.20 150000
-
 gel filtration Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.20 Pseudomonas sp. Q4R9M3
-
-
3.4.13.20 Pseudomonas sp. MCI3434 Q4R9M3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.13.20 proteolytic modification the mature enzyme with two polypeptide chains (alpha and beta) is formed by the cleavage of Gly238-Ser239 peptide bond of the 366-residue precursor Pseudomonas sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.13.20 recombinant enzyme is purified from the Escherichia coli JM109 harboring p2DAPEX with a recovery of 10.3% Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.13.20 beta-Ala-beta-Ala + H2O 48% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. beta-Ala + beta-Ala
-
 ?
3.4.13.20 beta-Ala-beta-Ala + H2O 48% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. MCI3434 beta-Ala + beta-Ala
-
 ?
3.4.13.20 beta-Ala-Gly + H2O 76% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. beta-Ala + Gly
-
 ?
3.4.13.20 beta-Ala-L-Ala + H2O preferred substrate Pseudomonas sp. beta-Ala + L-Ala
-
 ?
3.4.13.20 beta-Ala-L-His + H2O i.e. carnosine, 57% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. beta-Ala + L-His
-
 ?
3.4.13.20 beta-Ala-L-His + H2O i.e. carnosine, 57% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. MCI3434 beta-Ala + L-His
-
 ?
3.4.13.20 beta-Ala-L-Leu + H2O 49% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. beta-Ala + L-Leu
-
 ?
3.4.13.20 beta-Ala-NH2 + H2O 58% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. beta-Ala + NH3
-
 ?
3.4.13.20 D-Ala-4-nitroanilide + H2O 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 Pseudomonas sp. D-Ala + 4-nitroaniline
-
 ?
3.4.13.20 D-Ala-4-nitroanilide + H2O 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 Pseudomonas sp. MCI3434 D-Ala + 4-nitroaniline
-
 ?
3.4.13.20 D-Ala-NH2 + H2O 0.6% of the activity compared to beta-Ala-L-Ala Pseudomonas sp. D-Ala + NH3
-
 ?
3.4.13.20 L-Ala-4-nitroanilide + H2O 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 Pseudomonas sp. L-Ala + 4-nitroaniline
-
 ?
3.4.13.20 L-Ala-4-nitroanilide + H2O 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 Pseudomonas sp. MCI3434 L-Ala + 4-nitroaniline
-
 ?
3.4.13.20 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 Pseudomonas sp. ?
-
 ?
3.4.13.20 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 Pseudomonas sp. MCI3434 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.13.20 octamer alpha4beta4, 2 * 13000 + 2 * 27000, SDS-PAGE Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.4.13.20 DmpA
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.13.20 30
-
 assay at Pseudomonas sp.
3.4.13.20 60
-
-
 Pseudomonas sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.13.20 45
-
 10 min, stable below Pseudomonas sp.
3.4.13.20 50
-
 10 min, 13% loss of activity Pseudomonas sp.
3.4.13.20 55
-
 10 min, 51% loss of activity Pseudomonas sp.
3.4.13.20 60
-
 10 min, complete inactivation Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.13.20 8
-
 assay at Pseudomonas sp.
3.4.13.20 9 10
-
 Pseudomonas sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.13.20 6 11 30°C, 10 min, stable Pseudomonas sp.