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

BRENDA support

Literature summary for 2.7.7.99 extracted from

  • Gisin, J.; Schneider, A.; Naegele, B.; Borisova, M.; Mayer, C.
    A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis (2013), Nat. Chem. Biol., 9, 491-493 .
    View publication on PubMed
Search for more literature for 2.7.7.99

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q88QT2
-
-
Pseudomonas putida DSM 6125 Q88QT2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate Pseudomonas putida ?
-
 ?
additional information no substrates: N-acetyl-D-glucosamine 1-phosphate, N-acetyl-D-galactosamine 1-phosphate Pseudomonas putida DSM 6125 ?
-
 ?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
-
 Pseudomonas putida UDP-N-acetyl-alpha-D-muramate + diphosphate
-
 ?
UTP + N-acetyl-alpha-D-muramate 1-phosphate
-
 Pseudomonas putida DSM 6125 UDP-N-acetyl-alpha-D-muramate + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
murU
-
 Pseudomonas putida
N-acetylmuramate alpha-1-phosphate uridylyltransferase
-
 Pseudomonas putida
pp_0406
-
 Pseudomonas putida

General Information

General Information Comment Organism
physiological function enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity Pseudomonas putida