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BRENDA support

Ligand tobramycin

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Basic Ligand Information

Molecular Structure
Picture of tobramycin (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C18H37N5O9
tobramycin
NLVFBUXFDBBNBW-PBSUHMDJSA-N
Synonyms:
nebramycin factor 6, tobramicin

Related pathways


Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5' + AMP + diphosphate + phosphate
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (32 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
tobramycin + carbamoyl phosphate + ATP + H2O = nebramycin 5' + AMP + diphosphate + phosphate
show the reaction diagram
-
tobramycin/in + ATP + H2O = tobramycin/out + ADP + phosphate
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
tobramycin/in + ATP + H2O = tobramycin/out + ADP + phosphate
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
induces lon protease by subinhibitory concentrations
-

Inhibitor in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
about 40% residual activity at 1 mM
-
substrate inhibition
mixed competitive inhibition
-
pH-dependent inhibition
-
substrate inhibition, uncompetitive versus MgATP2-
-
non-competitive versus streptomycin and uncompetitive versus ATP
-
the inhibition by aminoglycosides appears to be due to substrate depletion caused by binding of aminoglycosides to the negatively charged phospholipid and can be overcome by raising the substrate concentration
-
slight inhibition of purified elastase
-
uncompetitive inhibition
-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (28 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
3.34
-
wild type enzyme, at pH 6.5 and 25°C

KM Value (36 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.186
-
wild type enzyme, at pH 6.5 and 25°C
0.001
-
above 0.001, pH 7.0, 22°C
0.00276
-
pH 9.0, 25°C

Ki Value (9 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0071
-
pH 7.4, 22°C
0.01
-
at pH 8.0, temperature not specified in the publication

IC50 Value (3 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.8
-
at pH 7.4 and 30°C
7.2
-
-
0.059
-
at pH 8.0, temperature not specified in the publication

References & Links

Links to other databases for tobramycin

EXTERNAL LINKS