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Literature summary for 2.3.1.60 extracted from

  • Williams, J.W.; Northrop, D.B.
    Substrate specificity and structure-activity relationships of gentamicin acetyltransferase I. The dependence of antibiotic resistance upon substrate Vmax/Km values (1978), J. Biol. Chem., 253, 5908-5914.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-deoxystreptamine weak Escherichia coli
amikacin i.e. BB-K 8 Escherichia coli
garamine
-
Escherichia coli
Kanamine
-
Escherichia coli
kanamycin A
-
Escherichia coli
kanamycin C
-
Escherichia coli
lividomycin
-
Escherichia coli
Lividomycin B
-
Escherichia coli
additional information inhibition kinetics Escherichia coli
neomycin best inhibitor Escherichia coli
paromomycin
-
Escherichia coli
Paromomycin I
-
Escherichia coli
ribostamycin
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic pattern Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
containing R-factor JR88
-
Escherichia coli C600
-
containing R-factor JR88
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + fortimicin A
-
Escherichia coli CoA + N2'-acetylfortimicin A
-
?
acetyl-CoA + gentamicin A
-
Escherichia coli CoA + N3'-acetylgentamicin A
-
?
acetyl-CoA + gentamicin B
-
Escherichia coli CoA + N3'-acetylgentamicin B
-
?
acetyl-CoA + gentamicin B1
-
Escherichia coli CoA + N3'-acetylgentamicin B1
-
?
acetyl-CoA + gentamicin C1
-
Escherichia coli CoA + N3'-acetylgentamicin C1
-
?
acetyl-CoA + gentamicin C1a best substrate Escherichia coli CoA + N3'-acetylgentamicin C1a
-
?
acetyl-CoA + gentamicin C1a enzyme modifies the 3-N-position of the deoxystreptamine ring Escherichia coli CoA + N3'-acetylgentamicin C1a
-
?
acetyl-CoA + gentamicin C1a best substrate Escherichia coli C600 CoA + N3'-acetylgentamicin C1a
-
?
acetyl-CoA + gentamicin C1a enzyme modifies the 3-N-position of the deoxystreptamine ring Escherichia coli C600 CoA + N3'-acetylgentamicin C1a
-
?
acetyl-CoA + gentamicin C2
-
Escherichia coli CoA + N3'-acetylgentamicin C2
-
?
acetyl-CoA + gentamicin XK62-2
-
Escherichia coli CoA + N3'-acetylgentamicin XK62-2
-
?
acetyl-CoA + kanamycin B
-
Escherichia coli CoA + N3'-acetylkanamycin B
-
?
acetyl-CoA + N-ethylsisomicin
-
Escherichia coli CoA + N3'-acetylethylsisomicin
-
?
acetyl-CoA + neamine
-
Escherichia coli CoA + N3'-acetylneamine
-
?
acetyl-CoA + nebramine
-
Escherichia coli CoA + N2'-acetylnebramine
-
?
acetyl-CoA + sisomicin best substrate Escherichia coli CoA + N3'-acetylsisomicin
-
?
acetyl-CoA + sisomicin best substrate Escherichia coli C600 CoA + N3'-acetylsisomicin
-
?
acetyl-CoA + tobramycin
-
Escherichia coli CoA + N3'-acetyltobramycin
-
?
acetyl-CoA + tobramycin
-
Escherichia coli C600 CoA + N3'-acetyltobramycin
-
?
additional information substrate structure/activity relationship Escherichia coli ?
-
?
additional information substrate structure/activity relationship Escherichia coli C600 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0004
-
neomycin
-
Escherichia coli
0.002
-
lividomycin
-
Escherichia coli
0.0036
-
garamine
-
Escherichia coli
0.0083
-
paromomycin
-
Escherichia coli
0.024
-
amikacin
-
Escherichia coli
0.026
-
kanamycin C
-
Escherichia coli
0.07
-
ribostamycin
-
Escherichia coli
0.093
-
kanamycin A
-
Escherichia coli
0.208
-
Kanamine
-
Escherichia coli
2
-
2-deoxystreptamine
-
Escherichia coli