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

BRENDA support

Literature summary for 6.3.2.8 extracted from

  • Jin, H.; Emanuele, J.J.; Fairman, R.; Robertson, J.G.; Hail, M.E.; Ho, H.T.; Falk, P.J.; Villafranca, J.J.
    Structural studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase (1996), Biochemistry, 35, 1423-1431.
    View publication on PubMed
Search for more literature for 6.3.2.8

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54486
-
 1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations Escherichia coli
54486
-
 2 * 54486, calculation from nucleotide sequence, electrospray mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-Ala Escherichia coli adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one essential step in cell wall biosynthesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramate + L-Ala
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala
-
 ?
ATP + UDP-N-acetylmuramate + L-Ala adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one essential step in cell wall biosynthesis Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 54486, calculation from nucleotide sequence, electrospray mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations Escherichia coli
monomer 1 * 54486, calculation from nucleotide sequence, electrospray ionization mass spectrometry, enzyme exists in equilibrium between monomeric and dimeric form, sedimentation equilibrium analysis at multiple speeds and multiple concentrations Escherichia coli