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

BRENDA support

Literature summary for 3.5.1.28 extracted from

  • Pennartz, A.; Genereux, C.; Parquet, C.; Mengin-Lecreulx, D.; Joris, B.
    Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme (2009), Antimicrob. Agents Chemother., 53, 2991-2997.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.28

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 x * 32000 Da, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P75820
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GlcNAc-anhydroMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala + H2O biphasic behavior: rapid exponential phase preceding a linear phase (0.027 mM substrate, 0.000106 mM enzyme) Escherichia coli GlcNAc-anhydroMurNAc + L-Ala-gamma-D-Glu-meso-diaminopimelyl-D-Ala
-
 ?

Subunits

Subunits Comment Organism
? x * 32000 Da, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
N-acetylmuramoyl-L-alanine amidase
-
 Escherichia coli