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Literature summary for 2.3.1.81 extracted from

  • Coombe, R.G.; George, A.M.
    Purification and properties of an aminoglycoside acetyltransferase from Pseudomonas aeruginosa (1982), Biochemistry, 21, 871-875.
    View publication on PubMed

General Stability

General Stability Organism
enzyme activity is significantly stabilized when preparations contain substrate Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
kanamycin A substrate inhibition Pseudomonas aeruginosa
tobramycin substrate inhibition Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000724
-
sisomicin pH 7.2, 34°C Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
-
Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
Vmax 0.102 (sisomicin), pH 7.2, 34°C Pseudomonas aeruginosa
9.743
-
pH 7.2, 34°C Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + sisomicin
-
Pseudomonas aeruginosa CoA + N3'-acetylsisomicin
-
?

Synonyms

Synonyms Comment Organism
AAC(3)
-
Pseudomonas aeruginosa
aminoglycoside 3-acetyltransferase
-
Pseudomonas aeruginosa