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Literature summary for 2.7.7.47 extracted from

  • Kono, M.; Ohmiya, K.; Kanda, T.; Noguchi, N.; O'Hara, K
    Purification and characterization of chromosomal streptomycin adenylyltransferase from derivatives of Bacillus subtilis Marburg 168 (1987), FEMS Microbiol. Lett., 40, 223-228.
No PubMed abstract available
Search for more literature for 2.7.7.47

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00008
-
 streptomycin pH 7.8, 37°C Bacillus subtilis
0.00032
-
 streptomycin pH 7.8, 37°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
chromosome
-
 Bacillus subtilis 5694
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
-
 Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + streptomycin Bacillus subtilis enzyme leads to resistance, destroys the inhibitory activity of streptomycin diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin Escherichia coli enzyme leads to resistance, destroys the inhibitory activity of streptomycin diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin Bacillus subtilis Marburg168 BD224 enzyme leads to resistance, destroys the inhibitory activity of streptomycin diphosphate + 3''-adenylylstreptomycin
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 Marburg168 BD224
-
Bacillus subtilis Marburg168 BD224
-
 Marburg168 BD224
-
Escherichia coli
-
 K12 W1895 HfrC
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.000046
-
 streptomycin Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + streptomycin
-
 Bacillus subtilis diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin
-
 Escherichia coli diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin enzyme leads to resistance, destroys the inhibitory activity of streptomycin Bacillus subtilis diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin enzyme leads to resistance, destroys the inhibitory activity of streptomycin Escherichia coli diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin
-
 Bacillus subtilis Marburg168 BD224 diphosphate + 3''-adenylylstreptomycin
-
 ?
ATP + streptomycin enzyme leads to resistance, destroys the inhibitory activity of streptomycin Bacillus subtilis Marburg168 BD224 diphosphate + 3''-adenylylstreptomycin
-
 ?
additional information does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase Bacillus subtilis ?
-
 ?
additional information does not adenylate spectinomycin, enzyme might be identical to AAD aminoglycoside 3''-adenylyltransferase Bacillus subtilis Marburg168 BD224 ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Bacillus subtilis
50
-
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Bacillus subtilis
9
-
-
 Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli isoelectric focusing
-
 5.2
Bacillus subtilis isoelectric focusing
-
 6