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Literature summary for 2.3.1.81 extracted from
- Thermodynamics of an aminoglycoside modifying enzyme with low substrate promiscuity The aminoglycoside N3 acetyltransferase-VIa (2017), Proteins, 85, 1258-1265 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Enterobacter cloacae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.002 | - |
gentamicin C1 | pH 7.6, 25°C | Enterobacter cloacae |  |
| 0.003 | - |
gentamicin C2 | pH 7.6, 25°C | Enterobacter cloacae | |
| 0.015 | - |
sisomicin | pH 7.6, 25°C | Enterobacter cloacae | |
| 0.0802 | - |
kanamycin B | pH 7.6, 25°C | Enterobacter cloacae | |
| 0.106 | - |
tobramycin | pH 7.6, 25°C | Enterobacter cloacae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Enterobacter cloacae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + gentamicin C1 | - |
Enterobacter cloacae | CoA + N3'-acetylgentamicin C1 | - |
? | |
| acetyl-CoA + gentamicin C2 | - |
Enterobacter cloacae | CoA + N3'-acetylgentamicin C2 | - |
? | |
| acetyl-CoA + kanamycin B | - |
Enterobacter cloacae | CoA + N3'-acetylkanamycin B | - |
? | |
| acetyl-CoA + sisomicin | - |
Enterobacter cloacae | CoA + N3'-acetyl-sisomicin | - |
? | |
| acetyl-CoA + tobramycin | - |
Enterobacter cloacae | CoA + N3'-acetyltobramycin | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| AAC-VIa | - |
Enterobacter cloacae |
| aminoglycoside N3-acetyltransferase-VIa | - |
Enterobacter cloacae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 9.7 | - |
gentamicin C1 | pH 7.6, 25°C | Enterobacter cloacae | |
| 14.5 | - |
kanamycin B | pH 7.6, 25°C | Enterobacter cloacae | |
| 18.4 | - |
gentamicin C2 | pH 7.6, 25°C | Enterobacter cloacae | |
| 24.5 | - |
sisomicin | pH 7.6, 25°C | Enterobacter cloacae | |
| 43.5 | - |
tobramycin | pH 7.6, 25°C | Enterobacter cloacae | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 200 | - |
kanamycin B | pH 7.6, 25°C | Enterobacter cloacae | |
| 400 | - |
tobramycin | pH 7.6, 25°C | Enterobacter cloacae | |
| 1600 | - |
sisomicin | pH 7.6, 25°C | Enterobacter cloacae | |
| 4700 | - |
gentamicin C1 | pH 7.6, 25°C | Enterobacter cloacae | |
| 6100 | - |
gentamicin C2 | pH 7.6, 25°C | Enterobacter cloacae | |
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