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Literature summary for 2.3.1.82 extracted from

  • Kim, C.; Hesek, D.; Zajicek, J.; Vakulenko, S.B.; Mobashery, S.
    Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3)-Ii/AAC(6)-IId from Serratia marcescens (2006), Biochemistry, 45, 8368-8377.
    View publication on PubMed

Inhibitors

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 [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

Organism UniProt Comment Textmining
Serratia marcescens
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
ANT(3'')-Ii/AAC(6')-IId bifunctional enzyme catalyzes adenylation and acetylation of aminoglycoside antibiotics Serratia marcescens

Turnover Number [1/s]

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 [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