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Literature summary for 3.5.1.28 extracted from

  • Uehara, T.; Park, J.T.
    An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli (2007), J. Bacteriol., 189, 5634-5641.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
-
Escherichia coli 19867
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required for activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O Escherichia coli
-
?
-
?
peptidoglycan + H2O 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.
1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
-
Escherichia coli ?
-
?
GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
-
Escherichia coli L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
-
?
peptidoglycan + H2O
-
Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
1,6-anhydro-N-acetylmuramic acid-L-alanine amidase
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9
-
Escherichia coli