Ligand puromycin

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of puromycin (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C22H29N7O5
puromycin
RXWNCPJZOCPEPQ-NVWDDTSBSA-N

Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (17 results)

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

Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L-homocysteine + puromycin
show the reaction diagram
-
-
ATP + H2O + puromycin/in = ADP + phosphate + puromycin/out
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
increases level of misfolded proteins, HtrA is required for growth under conditions in which misfolded proteins accumulate
-

Inhibitor in Enzyme-catalyzed Reactions (63 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
weak
-
prior incubation of ribosomes with puromycin inhibits both the binding and depurination by the enzyme
-
0.1 mM, 36% inhibition. 0.01 mM, 5% inhibition
-
54% inhibition at 1 mM
-
0.005 M: no effect, 0.025 M: complete inhibition, Ala-Gly-Ala-Gly synthesis
-
0.5 mM, 55% inhibition
-
1 mM, 17% inhibition
-
0.1 mM, 97% inhibition
-
peptidase inhibitor
-
competitive inhibition of hydrolysis L-Ala-4-nitroanilide
-
aminonucleoside antibiotic produced by Streptomyces alboniger, very weak inhibitor of AdT
-

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

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (2 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.17
-
at 37°C and pH 7.5
0.98
-
-

KM Value (2 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.1
-
at 37°C and pH 7.5
1.91
-
-

Ki Value (13 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
4.1
-
very weak inhibitor of AdT

IC50 Value (3 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.0031
-
IC50: 0.0031 mM, kidney enzyme

References & Links

Links to other databases for puromycin

ChEBI
PubChem
-
PubChem