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

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
3.5.1.28
-
 Escherichia coli

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.28 1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O Escherichia coli
-
 ?
-
 ?
3.5.1.28 peptidoglycan + H2O Escherichia coli
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.28 Escherichia coli P75820
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.28
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.28 1,6-anhydro-N-acetylmuramic acid-tripeptide + H2O
-
 Escherichia coli ?
-
 ?
3.5.1.28 GlcNAc-anhMurNAc-L-Ala-D-Glu-Dap + H2O
-
 Escherichia coli L-Ala-D-Glu-Dap + GlcNAc-anhMurNAc
-
 ?
3.5.1.28 peptidoglycan + H2O
-
 Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.28 1,6-anhydro-N-acetylmuramic acid-L-alanine amidase
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.28 4.5 9
-
 Escherichia coli