Inhibitors | Comment | Organism | Structure |
---|---|---|---|
6'-N-acetylkanamycin A | competitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA | Serratia marcescens | |
butyryl-CoA | uncompetitive versus kanamycin A and competitive versus acetyl CoA | Serratia marcescens | |
CoASH | uncompetitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA | Serratia marcescens | |
paromomycin | competitive versus kanamycin A and noncompetitive/mixed versus acetyl-CoA | Serratia marcescens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.012 | - |
kanamycin A | pH 7.5 | Serratia marcescens | |
0.015 | - |
gentamicin | pH 7.5 | Serratia marcescens | |
0.036 | - |
netilmicin | pH 7.5 | Serratia marcescens | |
0.044 | - |
acetyl-CoA | pH 7.5 | Serratia marcescens | |
0.313 | - |
amikacin | pH 7.5 | Serratia marcescens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Serratia marcescens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + amikacin | - |
Serratia marcescens | CoA + N6'-acetylamikacin | - |
? | |
acetyl-CoA + gentamicin | - |
Serratia marcescens | CoA + N6'-acetylgentamicin | - |
? | |
acetyl-CoA + kanamycin A | the bifunctional antibiotic resistance enzyme from Serratia marcescens catalyzes adenylation and acetylation of aminoglycoside antibiotics. The structure assignment of the enzymic products indicated that acetylation takes place on the 6'-amine of kanamycin A and the adenylation on 3''- and 9-hydroxyl groups of streptomycin and spectinomycin, respectively. The adenyltransferase domain appears to be highly specific to spectinomycin and streptomycin, while the acetyltransferase domain shows a broad substrate profile. Initial velocity patterns indicate that both domains follow a sequential kinetic mechanism | Serratia marcescens | CoA + N6'-acetylkanamycin A | - |
? | |
acetyl-CoA + netilmicin | - |
Serratia marcescens | CoA + N6'-acetylnetilmicin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ANT(3'')-Ii/AAC(6')-IId | bifunctional enzyme catalyzes adenylation and acetylation of aminoglycoside antibiotics | Serratia marcescens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
amikacin | pH 7.5 | Serratia marcescens | |
0.2 | - |
netilmicin | pH 7.5 | Serratia marcescens | |
0.5 | - |
gentamicin | pH 7.5 | Serratia marcescens | |
0.8 | - |
acetyl-CoA | pH 7.5 | Serratia marcescens | |
0.8 | - |
kanamycin A | pH 7.5 | Serratia marcescens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.025 | - |
butyryl-CoA | versus acetyl-CoA, K(is) | Serratia marcescens | |
0.04 | - |
6'-N-acetylkanamycin A | versus kanamycin A, K(is) | Serratia marcescens | |
0.042 | - |
CoASH | versus acetyl-CoA, K(is) | Serratia marcescens | |
0.043 | - |
CoASH | versus acetyl-CoA, K(ii) | Serratia marcescens | |
0.06 | - |
paromomycin | versus kanamycin A, K(is) | Serratia marcescens | |
0.069 | - |
CoASH | versus kanamycin A, K(ii) | Serratia marcescens | |
0.117 | - |
paromomycin | versus acetyl-CoA, K(is) | Serratia marcescens | |
0.145 | - |
paromomycin | versus acetyl-CoA, K(ii) | Serratia marcescens | |
0.15 | - |
6'-N-acetylkanamycin A | versus acetyl-CoA, K(is) | Serratia marcescens | |
0.188 | - |
butyryl-CoA | versus kanamycin A, K(ii) | Serratia marcescens | |
0.385 | - |
6'-N-acetylkanamycin A | versus acetyl-CoA, K(ii) | Serratia marcescens |