Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Inhibitors Comment Organism Structure
3.4.16.4 4-chloromercuribenzoate complete inhibition at 1 mM Priestia megaterium
3.4.16.4 benzylpenicillin 80% inhibition at 0.1 mg/ml Priestia megaterium
3.4.16.4 cefmetazole
-
 Priestia megaterium
3.4.16.4 Methicillin
-
 Priestia megaterium
3.4.16.4 nocardicin A
-
 Priestia megaterium
3.4.16.4 penicillin the enzyme is sensitive to inhibition, penicillin-binding profile during development of spores, overview Priestia megaterium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.16.4 Mg2+ required Priestia megaterium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.16.4 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
-
 ?
3.4.16.4 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

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.16.4 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.4 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
-
 ?
3.4.16.4 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

EC Number Subunits Comment Organism
3.4.16.4 More enzyme peptide mapping Priestia megaterium

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.16.4 37
-
 assay at Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.16.4 5.4
-
 vegetative and stage-V forespore membrane DD-carboxypeptidase Priestia megaterium