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Literature summary for 3.4.16.4 extracted from

  • Todd, J.A.; Ellar, D.J.
    Identification of penicillin-binding protein 5a of Bacillus megaterium KM as a DD-carboxypeptidase (1983), Biochem. J., 214, 653-655.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate complete inhibition at 1 mM Priestia megaterium
benzylpenicillin 80% inhibition at 0.1 mg/ml Priestia megaterium
cefmetazole
-
Priestia megaterium
Methicillin
-
Priestia megaterium
nocardicin A
-
Priestia megaterium
penicillin the enzyme is sensitive to inhibition, penicillin-binding profile during development of spores, overview Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Priestia megaterium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O Priestia megaterium i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O Priestia megaterium KM / ATCC 13632 i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
-
?

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-
Priestia megaterium KM / ATCC 13632
-
two isozymes penicillin-binding protein 5 and penicillin-binding protein 5a
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information during endospore development in Bacillus megaterium strain KM, unique sporulation-specific penicillin-binding proteins are synthesized and inserted into the forespore membranes, vegetative and stage-V forespore membrane DD-carboxypeptidase, penicillin-binding profile, overview Priestia megaterium
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate Priestia megaterium D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O i.e. UDP-N-acetylmuraminoyl-pentapeptide, release of D-alanine from UDPMurNAc-pentapeptide substrate Priestia megaterium KM / ATCC 13632 D-Ala + UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala
-
?

Subunits

Subunits Comment Organism
More enzyme peptide mapping Priestia megaterium

Synonyms

Synonyms Comment Organism
DD-Carboxypeptidase
-
Priestia megaterium
penicillin-binding protein 5
-
Priestia megaterium
penicillin-binding protein 5a
-
Priestia megaterium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
vegetative and stage-V forespore membrane DD-carboxypeptidase Priestia megaterium