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Literature summary extracted from

  • Gates, C.A.; Northrop, D.B.
    Determination of the rate-limiting segment of aminoglycoside nucleotidyltransferase 2''-I by pH- and viscosity-dependent kinetics (1988), Biochemistry, 27, 3834-3842.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.46 gentamycin C1
-
 Escherichia coli
2.7.7.46 netilmicin substrate inhibition Escherichia coli
2.7.7.46 sisomicin uncompetitive substrate inhibition Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.46 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.46 ATP + netilmicin C
-
 Escherichia coli diphosphate + 2''-adenylylnetilmicin C
-
 r
2.7.7.46 ATP + sisomicin
-
 Escherichia coli diphosphate + 2''-adenylylsisomicin
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.7.46 aminoglycoside nucleotidyltransferase 2''-I
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.46 6 9.5
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.46 0.154
-
 sisomicin
-
 Escherichia coli
2.7.7.46 1.84
-
 gentamycin C1
-
 Escherichia coli
2.7.7.46 5.12
-
 netilmicin
-
 Escherichia coli