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BRENDA support

Ligand kanamycin A

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Basic Ligand Information

Molecular Structure
Picture of kanamycin A (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C18H36N4O11
kanamycin A
SBUJHOSQTJFQJX-NOAMYHISSA-N
Synonyms:
kanamycin, kanamycin A, kanamycin[side 1], kanamycin[side 2]


Show all pahtways known for Show all BRENDA pathways known for kanamycin A

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2'-dehydrokanamycin A + NADPH + H+ = kanamycin A + NADP+
show the reaction diagram
-
UDP-alpha-D-kanosamine + 2'-deamino-2'-hydroxyneamine = UDP + kanamycin A
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (30 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
acetyl-CoA + kanamycin = CoA + N3''-acetylkanamycin
show the reaction diagram
-
ATP + kanamycin A = diphosphate + 2''-adenylylkanamycin A
show the reaction diagram
ATP + H2O + kanamycin[side 1] = ADP + phosphate + kanamycin[side 2]
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2'-dehydrokanamycin A + NADPH + H+ = kanamycin A + NADP+
show the reaction diagram
-
UDP-alpha-D-kanosamine + 2'-deamino-2'-hydroxyneamine = UDP + kanamycin A
show the reaction diagram
-
ATP + H2O + kanamycin[side 1] = ADP + phosphate + kanamycin[side 2]
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (24 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
about 70% residual activity at 1 mM
-
substrate inhibition
pH-dependent inhibition
-
50% inhibition by high nanomolar concentrations, competition with divalent metal ions
-
0.5 mg/ml
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
-

3D Structure of Enzyme-Ligand-Complex (PDB) (44 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (44 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
1.79
-
pH 7.5, 37°C, isoenzyme APH3'-IIIa

KM Value (51 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE

Ki Value (10 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.093
-
-
0.381
-
pH 7.6, 25°C
0.196
-
pH 6.0, 37°C

IC50 Value (2 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
3.8
-
at pH 7.4 and 30°C
20
-
-

References & Links

Links to other databases for kanamycin A

ChEBI
PubChem
ChEBI
PubChem