Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Taniguchi, K.; Nakamura, A.; Tsurubuchi, K.; O'Hara, K.; Sawai, T.
    The role of histidine residues conserved in the putative ATP-binding region of macrolide 2'-phosphotransferase II (2004), FEMS Microbiol. Lett., 232, 123-126.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.136 expression of wild-type and mutant enzymes in strains TG1 and N43 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.136 H198A site-directed mutagenesis, 50% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.1.136 H205A site-directed mutagenesis, 87.5% reduction of the minimal inhibitory concentration MIC level of oleandomycin and 50% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.1.136 H205N site-directed mutagenesis, unaffected minimal inhibitory concentration MIC level of oleandomycin, but more than 99% reduced activity compared to the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.136 oleandomycin
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.136 KCl
-
 Escherichia coli
2.7.1.136 Mg2+
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.136 Escherichia coli
-
 gene mphB
-
2.7.1.136 Escherichia coli CU1
-
 gene mphB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.136 recombinant wild-type and mutant enzymes from strain TG1 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.136 additional information
-
 substrate specificities of the mutant enzymes Escherichia coli
2.7.1.136 0.0007
-
 purified recombinant mutant H205A, substrate oleandomycin Escherichia coli
2.7.1.136 0.04
-
 purified recombinant wild-type enzyme, substrate roxithromycin or rokitamycin Escherichia coli
2.7.1.136 0.05
-
 purified recombinant wild-type enzyme, substrate josamycin or tylosin Escherichia coli
2.7.1.136 0.052
-
 purified recombinant mutant H198A, substrate oleandomycin Escherichia coli
2.7.1.136 0.056
-
 purified recombinant mutant H205N, substrate oleandomycin Escherichia coli
2.7.1.136 0.06
-
 purified recombinant wild-type enzyme, substrate troleandomycin, clarithromycin, azithromycin, or erythromycin Escherichia coli
2.7.1.136 0.1
-
 purified recombinant wild-type enzyme, substrate oleandomycin Escherichia coli
2.7.1.136 0.16
-
 purified recombinant wild-type enzyme, substrate kitasamycin Escherichia coli
2.7.1.136 0.21
-
 purified recombinant wild-type enzyme, substrate spiramycin Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.136 ATP + azithromycin 15-membered ring macrolide Escherichia coli ADP + azithromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + azithromycin 15-membered ring macrolide Escherichia coli CU1 ADP + azithromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + clarithromycin 14-membered ring macrolide Escherichia coli ADP + clarithromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + clarithromycin 14-membered ring macrolide Escherichia coli CU1 ADP + clarithromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + erythromycin 14-membered ring macrolide Escherichia coli ADP + erythromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + josamycin 15-membered ring macrolide Escherichia coli ADP + josamycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + kitasamycin 15-membered ring macrolide Escherichia coli ADP + kitasamycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + oleandomycin 14-membered ring macrolide Escherichia coli ADP + oleandomycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + oleandomycin 14-membered ring macrolide Escherichia coli CU1 ADP + oleandomycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + rokitamycin 15-membered ring macrolide Escherichia coli ADP + rokitamycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + roxithromycin 14-membered ring macrolide Escherichia coli ADP + roxithromycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + spiramycin 15-membered ring macrolide Escherichia coli ADP + spiramycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + spiramycin 15-membered ring macrolide Escherichia coli CU1 ADP + spiramycin 2'-O-phosphate
-
 ?
2.7.1.136 ATP + troleandomycin + H2O 14-membered ring macrolide Escherichia coli ADP + troleandomycin 2'-O-phosphate + acetate
-
 ?
2.7.1.136 ATP + tylosin 15-membered ring macrolide Escherichia coli ADP + tylosin 2'-O-phosphate
-
 ?
2.7.1.136 additional information substrate specificities of wild-type and mutant enzymes, structure-function considerations Escherichia coli ?
-
 ?
2.7.1.136 additional information substrate specificities of wild-type and mutant enzymes, structure-function considerations Escherichia coli CU1 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.136 macrolide 2'-phosphotransferase II
-
 Escherichia coli
2.7.1.136 MPH(2')
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.136 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.136 7.8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.136 ATP
-
 Escherichia coli