BRENDA - Enzyme Database

Interactions of coenzyme A with the aminoglycoside acetyltransferase (3)-IIIb and thermodynamics of a ternary system

Norris, A.L.; Serpersu, E.H.; Biochemistry 49, 4036-4042 (2010)

Data extracted from this reference:

KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.3.1.81
0.0154
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.0886
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.17
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.234
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.3.1.81
Pseudomonas aeruginosa
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.1.81
acetyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-acetylkanamycin A
-
-
-
?
2.3.1.81
acetyl-CoA + neomycin B
-
718871
Pseudomonas aeruginosa
CoA + N3-acetylneomycin B
-
-
-
?
2.3.1.81
malonyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-malonylkanamycin A
-
-
-
?
2.3.1.81
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
718871
Pseudomonas aeruginosa
?
-
-
-
-
2.3.1.81
n-propionyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-n-propionylkanamycin A
-
-
-
?
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.3.1.81
5.7
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
10.2
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
10.5
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
39.4
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.3.1.81
0.0154
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.0886
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.17
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
0.234
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.3.1.81
acetyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-acetylkanamycin A
-
-
-
?
2.3.1.81
acetyl-CoA + neomycin B
-
718871
Pseudomonas aeruginosa
CoA + N3-acetylneomycin B
-
-
-
?
2.3.1.81
malonyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-malonylkanamycin A
-
-
-
?
2.3.1.81
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
718871
Pseudomonas aeruginosa
?
-
-
-
-
2.3.1.81
n-propionyl-CoA + kanamycin A
-
718871
Pseudomonas aeruginosa
CoA + N3'-n-propionylkanamycin A
-
-
-
?
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.3.1.81
5.7
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
10.2
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
10.5
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
39.4
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.3.1.81
30
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
120
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
600
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
2600
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2.3.1.81
30
-
malonyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
120
-
n-propionyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
600
-
acetyl-CoA
cosubstrate neomycin B, pH 7.6, 25°C
Pseudomonas aeruginosa
2.3.1.81
2600
-
acetyl-CoA
cosubstrate kanamycin A, pH 7.6, 25°C
Pseudomonas aeruginosa