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Literature summary extracted from

  • Kumar, P.; Serpersu, E.
    Thermodynamics of an aminoglycoside modifying enzyme with low substrate promiscuity The aminoglycoside N3 acetyltransferase-VIa (2017), Proteins, 85, 1258-1265 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.81 expression in Escherichia coli Enterobacter cloacae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.81 0.002
-
gentamicin C1 pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 0.003
-
gentamicin C2 pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 0.015
-
sisomicin pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 0.0802
-
kanamycin B pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 0.106
-
tobramycin pH 7.6, 25°C Enterobacter cloacae

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.81 Enterobacter cloacae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.81 acetyl-CoA + gentamicin C1
-
Enterobacter cloacae CoA + N3'-acetylgentamicin C1
-
?
2.3.1.81 acetyl-CoA + gentamicin C2
-
Enterobacter cloacae CoA + N3'-acetylgentamicin C2
-
?
2.3.1.81 acetyl-CoA + kanamycin B
-
Enterobacter cloacae CoA + N3'-acetylkanamycin B
-
?
2.3.1.81 acetyl-CoA + sisomicin
-
Enterobacter cloacae CoA + N3'-acetyl-sisomicin
-
?
2.3.1.81 acetyl-CoA + tobramycin
-
Enterobacter cloacae CoA + N3'-acetyltobramycin
-
?
2.3.1.81 additional information binding of aminoglycosides to AAC-VIa is enthalpically favored and entropically disfavored with a net result of favorable Gibbs energy. A net deprotonation of the enzyme, ligand, or both accompanies the formation of binary and ternary complexes. Poor substrates: kanamycn A, ribostamycin, neomycin B Enterobacter cloacae ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.1.81 More AAC-VIa displays a monomer-dimer equilibrium in the absence of substrates.The dimer formation is concentration-dependent between 5 microM and 100 microM enzyme with more dimeric form appearing at higher concentrations. Binding of ligands shifts the enzyme to monomeric state Enterobacter cloacae

Synonyms

EC Number Synonyms Comment Organism
2.3.1.81 AAC-VIa
-
Enterobacter cloacae
2.3.1.81 aminoglycoside N3-acetyltransferase-VIa
-
Enterobacter cloacae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.81 9.7
-
gentamicin C1 pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 14.5
-
kanamycin B pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 18.4
-
gentamicin C2 pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 24.5
-
sisomicin pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 43.5
-
tobramycin pH 7.6, 25°C Enterobacter cloacae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.81 200
-
kanamycin B pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 400
-
tobramycin pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 1600
-
sisomicin pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 4700
-
gentamicin C1 pH 7.6, 25°C Enterobacter cloacae
2.3.1.81 6100
-
gentamicin C2 pH 7.6, 25°C Enterobacter cloacae