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Literature summary extracted from

  • McKay, G.A.; Wright, G.D.
    Catalytic mechanism of enterococcal kanamycin kinase (APH(3')-IIIa): viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism (1996), Biochemistry, 35, 8680-8685.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.95 overexpression of aminoglycoside phosphotransferase-IIIa, i.e. APH3'-IIIa in Escherichia coli Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.95 0.004
-
 kanamycin A pH 6.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 0.013
-
 kanamycin A pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 0.022
-
 ADP pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 0.028
-
 ATP pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 1.32
-
 3'-phosphokanamycin pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.95 ATP + kanamycin = ADP + kanamycin 3'-phosphate isoenzyme APH3'-IIIa follows a Theorell-Chance mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.95 ATP + kanamycin isoenzyme APH3'-IIIa Escherichia coli ADP + kanamycin 3'-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.7.1.95 aminoglycoside phosphotransferase 3'-IIIa, i.e. APH3'-IIIa
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.95 0.11
-
 ATP pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 1.76
-
 ATP pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli
2.7.1.95 1.79
-
 kanamycin A pH 7.5, 37°C, isoenzyme APH3'-IIIa Escherichia coli