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Literature summary for 5.4.2.8 extracted from

  • Naught, L.E.; Tipton, P.A.
    Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase (2001), Arch. Biochem. Biophys., 396, 111-118.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-Glucose 1,6-bisphosphate
-
Pseudomonas aeruginosa

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
glucose 1-phosphate substrate inhibition of reverse reaction Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-D-mannose 1-phosphate Pseudomonas aeruginosa
-
alpha-D-mannose 6-phosphate
-
r

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue, so that activity is reduced only 20fold from that of wild-type Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-D-glucose 1-phosphate
-
Pseudomonas aeruginosa alpha-D-glucose 6-phosphate
-
r
alpha-D-mannose 1-phosphate
-
Pseudomonas aeruginosa alpha-D-mannose 6-phosphate
-
r

Synonyms

Synonyms Comment Organism
PMM/PGM
-
Pseudomonas aeruginosa