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Literature summary for 2.3.1.81 extracted from

  • Norris, A.L.; Serpersu, E.H.
    Interactions of coenzyme A with the aminoglycoside acetyltransferase (3)-IIIb and thermodynamics of a ternary system (2010), Biochemistry, 49, 4036-4042.
    View publication on PubMed
Search for more literature for 2.3.1.81

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0154
-
 acetyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
0.0886
-
 n-propionyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
0.17
-
 acetyl-CoA cosubstrate neomycin B, pH 7.6, 25°C Pseudomonas aeruginosa
0.234
-
 malonyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + kanamycin A
-
 Pseudomonas aeruginosa CoA + N3'-acetylkanamycin A
-
 ?
acetyl-CoA + neomycin B
-
 Pseudomonas aeruginosa CoA + N3-acetylneomycin B
-
 ?
malonyl-CoA + kanamycin A
-
 Pseudomonas aeruginosa CoA + N3'-malonylkanamycin A
-
 ?
additional information CoASH associates with a high-affinity, catalytic site and with a secondary, low-affinity site that overlaps with the antibiotic binding pocket. The binding of CoASH to the high-affinity site occurs with a small, unfavorable enthalpy and a favorable entropy. Binding to the second site is highly exothermic and is accompanied by an unfavorable entropic contribution. The presence of an aminoglycoside alters the binding of CoASH to the enzyme dramatically such that the binding occurs with a favorable enthalpy and an unfavorable entropy. This is irrespective of which aminoglycoside is the cosubstrate and occurs without a significant change in the affinity of CoASH for the enzyme. The presence of antibiotics eliminates binding of CoASH to the second site Pseudomonas aeruginosa ?
-
 ?
n-propionyl-CoA + kanamycin A
-
 Pseudomonas aeruginosa CoA + N3'-n-propionylkanamycin A
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.7
-
 malonyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
10.2
-
 n-propionyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
10.5
-
 acetyl-CoA cosubstrate neomycin B, pH 7.6, 25°C Pseudomonas aeruginosa
39.4
-
 acetyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
30
-
 malonyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
120
-
 n-propionyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa
600
-
 acetyl-CoA cosubstrate neomycin B, pH 7.6, 25°C Pseudomonas aeruginosa
2600
-
 acetyl-CoA cosubstrate kanamycin A, pH 7.6, 25°C Pseudomonas aeruginosa