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Information on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase
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3.6.4.10 non-chaperonin molecular chaperone ATPaseIUBMB Comments
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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Word Map
- 3.6.4.10
-
client
- cytokine
- necrosis
- endothelial
- proteasome
- chaperonins
-
glucose-regulated
- breast
-
misfolded
-
chop
- cardiac
- ischemia
- lymphocyte
- caspase-3
- actin
- dismutase
-
refolding
- neurodegenerative
- artery
- sirnas
- autoimmune
-
cytoprotective
- myocardial
- epitope
- steroid
- bcl-2
- tnf
-
neuroprotective
- hypoxia
-
reperfusion
- immunogen
-
heat-induced
- mapks
- hyperthermia
- glucocorticoid
-
mycobacterial
-
anti-apoptotic
-
stressor
-
precondition
- infarct
-
stress-related
- cardiomyocytes
-
insult
-
tunel
-
perk
-
ischemia-reperfusion
- prion
-
cardioprotective
- chlamydia
- raf-1
- medicine
- drug development
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
hsp90, heat shock protein, grp78, hsp60, groel, molecular chaperone, hsc70, heat shock protein 70, heat shock protein 90, hsp40, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
70 kD heat shock protein
90-kDa heat shock protein
AAA+ chaperone
ATPase chaperone
BiP
chaperone hsp90
ClpB
ClpX
DnaK
DnaK chaperone
eukaryotic Hsc70 ATPase
Grp78
heat shock cognate protein
heat shock protein 70
heat shock protein 90
Hsc70
Hsp100
Hsp14.0
Hsp19.7
Hsp70
Hsp70 chaperone
Hsp70-1
Hsp70-2
Hsp90
Hsp90 molecular chaperone
HtpG
mitochondrial hsp70
molecular chaperone
mtHSP70
stress70 protein
DnaK
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
ClpB captures substrates on the upper surface of the AAA-1 ring before threading them through the ClpB hexamer in an ATP hydrolysis-driven step
-
ATP + H2O = ADP + phosphate
highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin
-
ATP + H2O = ADP + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-polymerizing)
This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins. They comprise a number of heat-shock-cognate proteins. They are also active in clathrin uncoating and in the oligomerization of actin.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + aggregated alpha-casein
ADP + phosphate + activated alpha-casein
-
-
-
?
ATP + H2O + aggregated fructose-1,6-bisphosphate aldolase
ADP + phosphate + activated fructose-1,6-bisphosphate aldolase
ATP + H2O + aggregated glucose-6-phosphate dehydrogenase
ADP + phosphate + activated glucose-6-phosphate dehydrogenase
ADP + ATP
ATP + ADP
-
transfer of gamma-phosphate with acid-stable autophosphorylation at residue T204 of the isolated ATPase domain
-
?
ATP + H2O
ADP + phosphate
-
ATP hydrolysis is the rate limiting step in the ATPase cycle of DnaK
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
210499, 210500, 210502, 210503, 210505, 210506, 210507, 210508, 210509, 210510, 210514, 210517, 654049, 654050, 654656, 656011, 657364, 668549, 684406, 696839, 697611, 701108, 701351, 734995, 755898, 757737, 758155, 758438
-
?
ATP + H2O
ADP + phosphate
-
ATP binding drives the chaperone in one direction and peptide binding pushes the chaperone back in the opposite direction (and thus increases Km)
-
?
ATP + H2O
ADP + phosphate
-
refolding of thermally denatured liciferase
-
?
ATP + H2O
ADP + phosphate
-
-
210507, 210508, 210512, 656160, 656348, 656552, 667113, 701351, 719075, 719344, 719653, 720049, 733348, 734233, 734536, 757440
-
?
ATP + H2O
ADP + phosphate
-
Hsp70 together with the two effector proteins Ydj1 and Sti1 exhibits chaperone activity towards luciferase. Sti1/Hop is essential for the transfer of non-native proteins from Hsp70 to Hsp90
-
?
ATP + H2O
ADP + phosphate
-
hsp90 is responsible for controlling the conformation, stability, activation, intracellular disposition, and proteolytic turnover of numerous important proteins that are involved in cell growth differentiation and survival
-
?
ATP + H2O
ADP + phosphate
-
HSP70 can bind to sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1a) and, depending on the severity of heat stress, protect SERCA1a function by stabilizing the nucleotide binding N-domain
-
?
ATP + H2O
ADP + phosphate
-
HSP70 can bind to sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1a) and, depending on the severity of heat stress, protect SERCA1a function by stabilizing the nucleotide binding N-domain
-
?
ATP + H2O
ADP + phosphate
-
-
210500, 210502, 210511, 210514, 210515, 210516, 654183, 656095, 656125, 656271, 667615, 668549, 700378, 701351, 719075, 734351, 756800, 757432, 757583, 757741
-
?
ATP + H2O
ADP + phosphate
-
Hsp104 mediates the solubilization of aggregated proteins in an ATP-dependent process assisted by the Hsp70/40 system. The affinity of Hsp104 toward polypeptides is regulated by nucleotides. In the presence of ATP or adenosine-5 -O -(3-thiotriphosphate), the chaperone forms complexes with reduced,carboxymethylated alpha-lactalbumin (RCMLa), a permanently unfolded model substrate. No binding is observed in the presence of ADP. The occupation of the N-terminally located nucleotide-binding domain with ATP seems to be crucial for substrate interaction. When ATP binding to this domain is impaired by mutation,Hsp104 loses its ability to interact with RCMLa. Upon association with a polypeptide,a conformational change occurs within Hsp104 that strongly reduces the dynamics of nucleotide exchange and commits the bound polypeptide to ATP hydrolysis
-
?
ATP + H2O
ADP + phosphate
-
SyClpC displays intrinsic chaperone activity in vitro, first by preventing aggregation of unfolded polypeptides and second by resolubilizing and refolding aggregated proteins into their native structures. The refolding activity of SyClpC is enhanced 3fold in presence of Bacillus subtilis ClpC adaptor protein MecA
-
?
ATP + H2O
ADP + phosphate
-
no correlation of a pronounced ATPase stimulation with chaperone activity using renaturation of GdnHCl denatured firefly luciferase
-
?
ATP + H2O
ADP + phosphate
-
hsp70A is highly inducible by heat shock and participates in asymmetric cell division
-
?
ATP + H2O + aggregated fructose-1,6-bisphosphate aldolase
ADP + phosphate + activated fructose-1,6-bisphosphate aldolase
-
-
-
?
ATP + H2O + aggregated fructose-1,6-bisphosphate aldolase
ADP + phosphate + activated fructose-1,6-bisphosphate aldolase
-
-
-
?
ATP + H2O + aggregated glucose-6-phosphate dehydrogenase
ADP + phosphate + activated glucose-6-phosphate dehydrogenase
-
-
-
?
ATP + H2O + aggregated glucose-6-phosphate dehydrogenase
ADP + phosphate + activated glucose-6-phosphate dehydrogenase
-
-
-
?
ATP + H2O + fluorescein isothiocyanatetagged-casein
ADP + phosphate + ?
-
-
?
ATP + H2O + fluorescein isothiocyanatetagged-casein
ADP + phosphate + ?
Leptospira interrogans Fiocruz L1-130
-
-
?
additional information
?
-
-
DnaK is very effective in preventing thermal aggregation of malate dehydrogenase
-
?
additional information
?
-
-
inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content
-
?
additional information
?
-
-
Hsp104 can unfold native protein structures such as green fluorescence protein fused to amino acid residues 1-70 of RepA if ATP and ATP-gammaS are present. No cochaperones are required
-
?
additional information
?
-
-
functional coupling of both chaperones ClpB and DnaK depends on specific properties of the client protein they interact with
-
-
additional information
?
-
-
NEF binding stabilizes the ATPase domain in an open form and thereby facilitates the nucleotide exchange step of the chaperone cycle
-
?
additional information
?
-
-
development and optimization of an ion exchange liquid chromatography method for the determination of ATP, ADP and AMP, for the direct separation, identification and determination of the adenosine nucleotides using a small disk shaped monolithic ethylenediamine column, specifically aimed at the determination of the ATP-ase activity of human heat shock protein 90, Hsp90, detailed overview
-
?
additional information
?
-
mortalin interacts with adenosine nucleotides with high affinity
-
?
additional information
?
-
-
mortalin interacts with adenosine nucleotides with high affinity
-
?
additional information
?
-
-
the N-terminal domain is dispensable for oligomerization, ATPase activity and prevention of aggregation activity of the enzyme
-
-
additional information
?
-
-
the imsHsp70 isoform is supposed to interact with translocating preproteins in pea chloroplasts
-
?
additional information
?
-
association between ClpB and DnaK at the protein aggregate surface, the substrate-binding domain of DnaK regulates ClpB dynamics
-
?
additional information
?
-
PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones
-
?
additional information
?
-
-
PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones
-
?
additional information
?
-
-
regulation of Hsp70 Ssa chaperone ATP hydrolysis is involved in prion propagation
-
?
additional information
?
-
-
Hsp104 actively unfolds its substrates during processing
-
?
additional information
?
-
-
Hsp104 can unfold native protein structures such as green fluorescence protein fused to amino acid residues 1-70 of RepA if ATP and ATP-gammaS are present. No cochaperones are required
-
?
additional information
?
-
-
effect of nucleotides on the formation of the cross-linked adduct: addition of ATP or ADP after formation of the mtHsp70-Hep1 complex leads to release and addition of ATPgammaS to partial release of mtHsp70 from Hep1, whereas almost no mtHsp70 dissociates from Hep1 upon addition of AMP-PNP
-
?
additional information
?
-
-
the enzyme collaborates with the Hsp70 chaperone system to dissolve protein aggregates both in vivo and in vitro
-
-
additional information
?
-
-
following its assembly, the Fe-S cluster is transferred from the Isu scaffold to a recipient protein. Transfer requires the Hsp70 chaperone system consisting of Hsp70 Ssq1, J-protein cochaperone Hsc20, and nucleotide exchange factor Mge1
-
-
additional information
?
-
-
the enzyme unfolds GFP-X30-H6,GFP-X7-H6, and GFP-15 with Km values of 0.0018 mM, 0.0052 mM, and 0.0016 mM, respectively
-
-
additional information
?
-
-
Hsp14.0 exists as a spherical 24-meric oligomer showing molecular chaperone activity, e.g. to protect thermophilic 3-isopropylmalate dehydrogenase from thermal aggregation at 87°C, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles and lacks molecular chaperone activity
-
?
additional information
?
-
-
Hsp14.0 exists as a spherical 24-meric oligomer showing molecular chaperone activity, e.g. to protect thermophilic 3-isopropylmalate dehydrogenase from thermal aggregation at 87°C, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles and lacks molecular chaperone activity
-
?
additional information
?
-
-
enzyme forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a chaperone in cooperation with KJE and ATP under poststress conditions
-
?
additional information
?
-
-
the hexameric, nonstress form of ClpB reactivates heat-aggregated proteins dependent on the DnaK system and ATP. The mixture of dimer and monomer, which is formed under stress conditions, protects substrate proteins from thermal inacivation and aggregation
-
?
additional information
?
-
the enzyme collaborates with the DnaK chaperone system to dissolve protein aggregates both in vivo and in vitro
-
-
additional information
?
-
the enzyme unfolds GFP-X30-H6,GFP-X7-H6, and GFP-15 with Km values of 0.0041 mM, 0.003 mM, and 0.0012 mM, respectively
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
210499, 210500, 210502, 210503, 210505, 210506, 210507, 210508, 210509, 210510, 210514, 210517, 654049, 654050, 654656, 656011, 657364, 734995, 755898, 757737, 758155, 758438
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
Hsp70 together with the two effector proteins Ydj1 and Sti1 exhibits chaperone activity towards luciferase. Sti1/Hop is essential for the transfer of non-native proteins from Hsp70 to Hsp90
-
-
?
ATP + H2O
ADP + phosphate
-
hsp90 is responsible for controlling the conformation, stability, activation, intracellular disposition, and proteolytic turnover of numerous important proteins that are involved in cell growth differentiation and survival
-
-
?
ATP + H2O
ADP + phosphate
-
-
210500, 210502, 210511, 210514, 210515, 210516, 654183, 656095, 656125, 656271, 734351, 756800, 757432, 757583, 757741
-
-
?
ATP + H2O
ADP + phosphate
-
hsp70A is highly inducible by heat shock and participates in asymmetric cell division
-
-
?
additional information
?
-
-
inactivation of the clpC1 gene encoding a chloroplast Hsp100 molecular chaperone causes growth retardation, leaf chlorosis, lower photosynthetic activity, and a specific reduction in photosystem content
-
-
?
additional information
?
-
-
NEF binding stabilizes the ATPase domain in an open form and thereby facilitates the nucleotide exchange step of the chaperone cycle
-
-
?
additional information
?
-
-
the imsHsp70 isoform is supposed to interact with translocating preproteins in pea chloroplasts
-
-
?
additional information
?
-
association between ClpB and DnaK at the protein aggregate surface, the substrate-binding domain of DnaK regulates ClpB dynamics
-
-
?
additional information
?
-
PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones
-
-
?
additional information
?
-
-
PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones
-
-
?
additional information
?
-
-
regulation of Hsp70 Ssa chaperone ATP hydrolysis is involved in prion propagation
-
-
?
additional information
?
-
-
the enzyme collaborates with the Hsp70 chaperone system to dissolve protein aggregates both in vivo and in vitro
-
-
-
additional information
?
-
-
enzyme forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a chaperone in cooperation with KJE and ATP under poststress conditions
-
-
?
additional information
?
-
the enzyme collaborates with the DnaK chaperone system to dissolve protein aggregates both in vivo and in vitro
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
additional information
-
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
additional information
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
additional information
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
additional information
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
additional information
Hsp70s invariably require a J-domain protein and, almost always, a nucleotide exchange factor (e.g., GrpE) as partners in order to be completely functional
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1aR,2Z,4E,6Z,14R)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylacetyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
-
-
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-6-([[(dimethylamino)acetyl]oxy]imino)-9,11-dihydroxy-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-(methylimino)-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylcarbonyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-6-(hydroxyimino)-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
(1aS,2Z,15R,16aR)-9-chloro-10,12-dihydroxy-15-methyl-1a,15,16,16a-tetrahydro-1H-7,4-(metheno)cyclopropa[h][12,2,3,4]benzoxatriazacyclopentadecin-13(8H)-one
-
-
(1R)-2-(5-chloro-2,4-dihydroxybenzoyl)-N-ethyl-2,3-dihydro-1H-isoindole-1-carboxamide
-
-
(3R,5E,9E,11Z)-13-chloro-7,14,16-trihydroxy-3-methyl-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(3S)-14,16-dihydroxy-3-methyl-3,4,5,6,9,10,11,12-octahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-amino-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
IPI-493
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[benzyl(ethyl)amino]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-20-chloro-13,19-dihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
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(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-9-(carbamoyloxy)-13,20,22-trihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-N-(prop-2-en-1-yl)-2-azabicyclo[16.3.1]docosa-1(22),4,6,10,18,20-hexaen-19-aminium chloride
(4E,6Z,8S,9S,10E,12S,13R,14S,16S,17R)-22-hydroxy-8,13,14,17-tetramethoxy-4,10,12,16,20-pentamethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
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-
(4E,8S,9S,10E,12S,13R,14S,16R)-13,20-dihydroxy-8,14-dimethoxy-10,12,16-trimethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(22),4,10,18,20-pentaen-9-yl carbamate
(5-[4-amino-6-[(2-methoxyphenyl)sulfanyl]-1,3,5-triazin-2-yl]-2,4-dichlorophenoxy)acetonitrile
-
-
(5E)-5-[(1-benzyl-1H-indol-3-yl)methylidene]-1-(2-fluorocyclohexyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5E,9E,11Z)-13-chloro-14,16-dihydroxy-11-[[(piperidin-1-ylacetyl)oxy]imino]-3,4,7,8,11,12-hexahydro-1H-2-benzoxacyclotetradecin-1-one
-
-
(5Z)-7-[4-fluoro-2-(pyridin-3-yl)phenyl]-5-(hydroxyimino)-4-methyl-5,6,7,8-tetrahydropyrido[4,3-d]pyrimidin-2-amine
-
-
(7R)-2-amino-7-[5-(6-methoxypyrazin-2-yl)-1,3-thiazol-4-yl]-4-methyl-7,8-dihydropyrido[4,3-d]pyrimidin-5(6H)-one
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-
1,3-dihydro-2H-isoindol-2-yl[6-hydroxy-3-(3-methylbenzyl)-1H-indazol-5-yl]methanone
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-
1-(3H-imidazo[4,5-c]pyridin-2-yl)-2,3-dihydro-5H-pyrrolo[2,1-a]isoindol-5-one
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1-(4-aminoquinazolin-6-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indol-4-one
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1-(5-ethyl-2,4-dihydroxyphenyl)-5-(trifluoromethyl)-1,3-dihydro-2H-benzimidazol-2-one
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1-(6-amino-9H-purin-8-yl)-3,6,6-trimethyl-1,5,6,7-tetrahydro-4H-indazol-4-one
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1-[4-(2-[6-amino-8-[(7-bromo-2,3-dihydro-1,4-benzodioxin-6-yl)sulfanyl]-3H-purin-3-yl]ethyl)piperidin-1-yl]-2-hydroxy-2-methylpropan-1-one
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17-allylamino-17-demethoxygeldanamycin
i.e. tanespimycin, binding kinetics, overview
2'-methoxy-5-[4-(2-methoxyethyl)-4H-1,2,4-triazol-3-yl]-5'-(propan-2-yl)biphenyl-2,4-diol
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-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-pentylbenzamide
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-
2,4-dihydroxy-5-[5-hydroxy-4-(2-methylphenyl)-4H-1,2,4-triazol-3-yl]-N-methyl-N-[2-(3-methylphenyl)ethyl]benzamide
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-
2,4-dihydroxy-N-methyl-N-(3-methylbenzyl)-5-[1-(2-methylphenyl)-1H-pyrazol-5-yl]benzamide
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-
2-(5-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-hydroxy-4H-1,2,4-triazol-4-yl]-1H-indol-1-yl)ethyl dihydrogen phosphate
-
-
2-([3-[2-(dimethylamino)ethoxy]-4-methoxyphenyl]amino)-4-(3,6,6-trimethyl-4-oxo-4,5,6,7-tetrahydro-1H-indazol-1-yl)benzamide
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-
2-amino-4-chloro-8-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-5-propyl-7,8-dihydropteridin-6(5H)-one
-
-
2-amino-4-[2,4-dichloro-5-[3-(pyrrolidin-1-yl)propoxy]phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide
-
NVP-BEP800/VER-82576
2-amino-6-benzyl-4-(2,4-dichlorophenyl)-5,6-dihydro-7H-pyrrolo[3,4-d]pyrimidin-7-one
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-
2-amino-6-chloro-9-[(4-iodo-3,5-dimethylpyridin-2-yl)methyl]-7-[2-(1H-pyrrol-1-yl)ethyl]-7,9-dihydro-8H-purin-8-one
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-
2-amino-N-ethyl-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
SNX-7081, weak inhibitor
2-fluoro-6-(tetrahydro-2H-pyran-4-ylamino)-4-(2,3,6,6-tetramethyl-4-oxo-4,5,6,7-tetrahydro-1H-indol-1-yl)benzamide
-
-
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide
-
-
2-[(6-bromo-1,3-benzodioxol-5-yl)methyl]-1-methyl-5-(propanoylamino)-1H-imidazole-4-carboxamide
-
-
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxycyclohexyl)quinazolin-4(3H)-one
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-
2-[2-[(4-methoxy-3,5-dimethyl-3,4-dihydropyridin-2-yl)methyl]-7,8-dihydro-2H-6-thia-1,2,3,5-tetraazaacenaphthylen-7-yl]-N-(5-methyl-1,3-thiazol-2-yl)acetamide
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2-[4-(1-methyl-1H-indol-5-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)pyridine-3,5-diol
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-
2-[6-amino-2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9H-purin-9-yl]ethyl sulfamate
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-
2-[6-amino-8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-N-hydroxyacetamide
-
-
2-[[4-(2-chloro-5-hydroxy-4-methoxyphenyl)-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-2-yl]sulfanyl]-N,N-dimethylacetamide
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-
2-[[5-(1,3-benzodioxol-5-yl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1-phenylethanone
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-
2-[[6-(dimethylamino)-1,3-benzodioxol-5-yl]sulfanyl]-1-[2-[(2,2-dimethylpropyl)amino]ethyl]-1H-imidazo[4,5-c]pyridin-4-amine
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CUDC-305
3,6-diamino-5-cyano-4-(4-methoxy-3-[[3-(trifluoromethyl)benzoyl]amino]phenyl)thieno[2,3-b]pyridine-2-carboxamide
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-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-fluorophenyl)-4H-pyrazole-4-carboxamide
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-
3-(5-chloro-2,4-dihydroxyphenyl)-N-(4-methoxyphenyl)-4H-pyrazole-4-carboxamide
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-
3-(5-chloro-2,4-dihydroxyphenyl)-N-[3-(trifluoromethyl)phenyl]-4H-pyrazole-4-carboxamide
-
-
3-(cyclopentylmethyl)-6-hydroxy-N-methyl-N-[4-(morpholin-4-yl)phenyl]-1H-indazole-5-carboxamide
-
-
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
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-
4-(2,4-dichloro-5-methoxyphenyl)-2-[2-(diethylamino)ethoxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
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-
4-(4-[4-methoxy-3-[methyl(2-methylpropyl)amino]phenyl]-5-sulfanyl-4H-1,2,4-triazol-3-yl)-6-(propan-2-yl)benzene-1,3-diol
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4-(but-2-yn-1-yl)-6-[4-(4-methoxyphenyl)-5-methyl-1,2-oxazol-3-yl]benzene-1,3-diol
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4-([2-carbamoyl-5-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]phenyl]amino)cyclohexyl glycinate
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SNX-5422
4-([2-[3,5-bis(trifluoromethyl)phenyl]-4,5-bis(4-methoxyphenyl)-1H-imidazol-1-yl]methyl)benzoic acid
-
inhibits the ATPase activity of Hsc70 by binding to its ATPase domain
4-amino-11,18,20-trimethyl-7-thia-3,5,11,15-tetraazatricyclo[15.3.1.12,6]docosa-1(21),2(22),3,5,17,19-hexaene-10,16-dione
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4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
4-ethyl-6-[4-(4-methoxynaphthalen-1-yl)-5-sulfanyl-4H-1,2,4-triazol-3-yl]benzene-1,3-diol
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4-[2-amino-4-chloro-7-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-7H-pyrrolo[2,3-d]pyrimidin-5-yl]but-3-yn-1-ol
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4-[4-(1,3-benzodioxol-5-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
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-
4-[4-(1-methyl-1H-indol-5-yl)-5-[(pyridin-3-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
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4-[4-(2-fluorophenyl)-5-hydroxy-4H-1,2,4-triazol-3-yl]-6-(2-phenylethyl)benzene-1,3-diol
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4-[4-(6-fluoro-1H-benzimidazol-2-yl)-9H-carbazol-9-yl]-2-[(trans-4-hydroxycyclohexyl)amino]benzamide
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4-[4-(diethylamino)phenyl]-5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-1,2-oxazole-3-carboxamide
4-[5-hydroxy-4-(1-methyl-1H-indol-5-yl)-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
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-
4-[5-hydroxy-4-[4-(morpholin-4-yl)phenyl]-4H-1,2,4-triazol-3-yl]-6-(propan-2-yl)benzene-1,3-diol
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-
4-[6,6-dimethyl-4-oxo-3-(trifluoromethyl)-3a,4,5,6,7,7a-hexahydro-1H-indazol-1-yl]-2-[(4-hydroxycyclohexyl)amino]benzamide
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SNX-2112
5-(5-ethyl-2,4-dihydroxyphenyl)-1-(naphthalen-1-yl)-1,3-dihydro-2H-imidazol-2-one
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-
5-amino-1-(5-aminopentyl)-2-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-1H-imidazole-4-carboxamide
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-
5-amino-1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]-1H-imidazole-4-carboxamide
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5-hydroxy-4-[5-hydroxy-4-[6-(morpholin-4-yl)pyridin-3-yl]-4H-1,2,4-triazol-3-yl]-2-(propan-2-yl)phenyl dihydrogen phosphate
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5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
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5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
6-bromo-N-[4-(quinolin-3-yl)-9H-fluoren-9-yl]-1,8a-dihydropyrido[2,3-d]pyrimidine-5-carboxamide
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6-[5-[(benzyloxy)carbonyl]-4-(4-cyclohexylphenyl)-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
-
IC50 value about 0.12-0.2 mM
6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
-
IC50 value about 0.12-0.2 mM
7-[2,4-dichloro-6-[2-(1H-pyrazol-1-yl)ethoxy]phenyl][1,3]thiazolo[5,4-d]pyrimidin-5-amine
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8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
9-[2-[(2,2-dimethylpropyl)amino]ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
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Apg2
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at high concentration (0.002 mM), Agp2 inhibits the ATPase activity of the enzyme
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cyclohexyl 5-[6-amino-8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl]-L-norvalinate
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diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
ethyl (4-[3-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-5-sulfanyl-4H-1,2,4-triazol-4-yl]benzyl)carbamate
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ethyl 2-amino-4-(4-bromo-2-chloro-5-methoxyphenyl)-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidine-6-carboxylate
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ethyl 4-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-6-methyl-2-oxo-1,2-dihydropyrimidine-5-carboxylate
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Guanidinium chloride
-
approx. 50% uncompetitive inhibition above 0.5 mM
methyl (2E)-3-[2-amino-4-(1,3-dihydro-2H-isoindol-2-ylcarbonyl)quinazolin-6-yl]prop-2-enoate
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methyl 4-(naphthalen-2-yl)-2-oxo-6-(phenoxymethyl)-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
IC50 value about 0.12 -0.2 mM
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-4H-pyrazole-4-carboxamide
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N-benzyl-6-(3-[[(2,6-dichloro-9H-purin-9-yl)acetyl]amino]-8-azabicyclo[3.2.1]oct-8-yl)pyridine-3-carboxamide
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N-butyl-2,4-dihydroxy-5-[(5-hydroxy-1,3-dihydro-2H-isoindol-2-yl)carbonyl]benzamide
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N-[2-(dimethylamino)ethyl]-6-[3-[(4-methoxy-2-methylbenzoyl)amino]-8-azabicyclo[3.2.1]oct-8-yl]pyridine-3-carboxamide
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N-[4-(3H-imidazo[4,5-c]pyridin-2-yl)-9H-fluoren-9-yl]quinoline-5-carboxamide
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N-[4-(aminosulfonothioyl)benzyl]-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
Sti1
-
co-chaperone, almost complete non-competitive inhibition at a 6fold excess of Sti1 in the presence of 80 mM KCL
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[(2R)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl](1,3-dihydro-2H-isoindol-2-yl)methanone
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[1-(3-bromo-4-cyanophenyl)-2-oxo-2,4,5,6,7,7a-hexahydro-1H-indol-3-yl]acetic acid
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[2,4-dihydroxy-5-(propan-2-yl)phenyl](5-[[methyl(piperidin-1-yl)amino]methyl]-1,3-dihydro-2H-isoindol-2-yl)methanone
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AT-13387
[4-[(2S)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl]phenyl](3,3-difluoropyrrolidin-1-yl)methanone
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-6-([[(dimethylamino)acetyl]oxy]imino)-9,11-dihydroxy-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-6-([[(dimethylamino)acetyl]oxy]imino)-9,11-dihydroxy-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-(methylimino)-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-(methylimino)-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylcarbonyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-14-methyl-6-[[(piperidin-1-ylcarbonyl)oxy]imino]-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-6-(hydroxyimino)-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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KF25706
(1aR,2Z,4E,6Z,14R,15aR)-8-chloro-9,11-dihydroxy-6-(hydroxyimino)-14-methyl-1a,6,7,14,15,15a-hexahydro-12H-oxireno[e][2]benzoxacyclotetradecin-12-one
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KF25706
(3S)-14,16-dihydroxy-3-methyl-3,4,5,6,9,10,11,12-octahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
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-
(3S)-14,16-dihydroxy-3-methyl-3,4,5,6,9,10,11,12-octahydro-1H-2-benzoxacyclotetradecine-1,7(8H)-dione
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-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
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(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[benzyl(ethyl)amino]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-19-[(4-[[benzyl(ethyl)amino]methyl]benzoyl)amino]-13-hydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3,20,22-trioxo-2-azabicyclo[16.3.1]docosa-1(21),4,6,10,18-pentaen-9-yl carbamate
-
-
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-9-(carbamoyloxy)-13,20,22-trihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-N-(prop-2-en-1-yl)-2-azabicyclo[16.3.1]docosa-1(22),4,6,10,18,20-hexaen-19-aminium chloride
-
IPI-504
(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-9-(carbamoyloxy)-13,20,22-trihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-3-oxo-N-(prop-2-en-1-yl)-2-azabicyclo[16.3.1]docosa-1(22),4,6,10,18,20-hexaen-19-aminium chloride
-
IPI-504
(4E,8S,9S,10E,12S,13R,14S,16R)-13,20-dihydroxy-8,14-dimethoxy-10,12,16-trimethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(22),4,10,18,20-pentaen-9-yl carbamate
-
KOSN1559
(4E,8S,9S,10E,12S,13R,14S,16R)-13,20-dihydroxy-8,14-dimethoxy-10,12,16-trimethyl-3-oxo-2-azabicyclo[16.3.1]docosa-1(22),4,10,18,20-pentaen-9-yl carbamate
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KOSN1559
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
-
-
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
-
-
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
PU-DZ8
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
-
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
PU-DZ8
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxyphenyl)quinazolin-4(3H)-one
-
micromolar inhibitor
2-[(E)-2-(2-hydroxy-3-methoxyphenyl)ethenyl]-3-(4-methoxyphenyl)quinazolin-4(3H)-one
-
micromolar inhibitor
3-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1H-pyrazole-5-carboxamide
-
VER-49009
3-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1H-pyrazole-5-carboxamide
-
VER-49009
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
-
-
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
-
-
4-(1,3-benzodioxol-5-yl)-3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazole-5-carboxylic acid
-
G3129
4-(1,3-benzodioxol-5-yl)-3-(5-ethyl-2,4-dihydroxyphenyl)-1H-pyrazole-5-carboxylic acid
-
G3129
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-(5-[[2-(morpholin-4-yl)ethyl]amino]-1,2-benzoxazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-(5-[[2-(morpholin-4-yl)ethyl]amino]-1,2-benzoxazol-3-yl)benzene-1,3-diol
-
-
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
-
CCT072440
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
-
CCT072440
4-ethyl-6-[4-(1H-imidazol-4-yl)-1H-pyrazol-3-yl]benzene-1,3-diol
-
G3130
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
-
CCT08159/RBT0028535
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
-
CCT08159/RBT0028535
4-[4-(2-methyl-1,3-thiazol-4-yl)-5-(trifluoromethyl)-1,2-oxazol-3-yl]benzene-1,3-diol
-
micromolar inhibitor
4-[4-(2-methyl-1,3-thiazol-4-yl)-5-(trifluoromethyl)-1,2-oxazol-3-yl]benzene-1,3-diol
-
micromolar inhibitor
4-[4-(4-benzylpiperazin-1-yl)-1H-pyrazol-3-yl]-6-chlorobenzene-1,3-diol
-
-
4-[4-(diethylamino)phenyl]-5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-1,2-oxazole-3-carboxamide
-
-
4-[4-(diethylamino)phenyl]-5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-1,2-oxazole-3-carboxamide
-
-
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
-
VER-50589
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
-
VER-50589
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
-
VER-52296/NVP-AUY922
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
-
NVP-AUY922
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-N-ethyl-4-[4-(morpholin-4-yl)phenyl]-1,2-oxazole-3-carboxamide
-
VER-52296/NVP-AUY922
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
-
CNF-2024/BIIB021
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
-
-
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
-
-
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
PU24FCl
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
PU24FCl
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
-
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
potent Hsp90 binder
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
-
potent Hsp90 binder
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
PU-H71
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
-
PU-H71
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
-
-
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
-
-
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
-
-
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
-
-
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
-
-
9-[2-(tert-butylamino)ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[2-(tert-butylamino)ethyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
-
-
ADP
-
complete loss of enzyme ATPase activity is seen at 0.5 mM ADP. Under saturating levels of ATP (5 mM), the enzyme loses more than 80% of its ATPase activity upon addition of as low a concentration as 0.25 mM ADP
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
-
-
geldanamycin
a competitive inhibitor of Hsp90 that binds to the ATP-binding pocket in the N-terminal domain of Hsp90 with a higher affinity than ATP, binding kinetics, overview
geldanamycin
-
inhibits hsp90 function in vitro at low micromolar concentrations via the interaction with the N-terminal ATP-binding domain of Hsp90, which results in destabilization of oncogenic client proteins via the proteasomal degradation pathway
goniothalamin
-
a naturally occurring styryl-lactone, that increases both Km and kcat of Hsp90, it binds to the N-terminal domain of Hsp90 activates its ATPase activity, while inhibiting the chaperone function of Hsp90
goniothalamin
-
inhibits the chaperone activity of the enzyme Hsp90
goniothalamin
-
a naturally occurring styryl-lactone, isolated from the air-dried bark of Goniothalamus tapis Miq., that increases both Km and kcat of Hsp90. Goniothalamin binds to the N-terminal domain of HtpG. Goniothalamin does not influence the interaction of HtpG with a non-native protein or the anti-aggregation activity of HtpG significantly. But it inhibits the activity of HtpG that assists refolding of a non-native protein in cooperation with the Hsp70 chaperone system. Goniothalamin does not inhibit the refolding assisted by the DnaK chaperone system indicating that goniothalamin exerts an inhibitory effect only on the HtpG-assisted refolding process
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
N-(4-acetylphenyl)-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
N-[4-(aminosulfonothioyl)benzyl]-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
N-[4-(aminosulfonothioyl)benzyl]-3-(5-chloro-2,4-dihydroxyphenyl)-1H-pyrazole-4-carboxamide
-
-
p23 protein
-
cochaperone, interacts with Hsp90 in both the absence and presence of nucleotide, with a higher affinity in presence of the ATP analogue 5'-adenylyl-beta,gamma-imidodiphosphate. Mixed inhibition, one p23 binds to each subunit of the Hsp90 dimer. Complex formation between Hsp90 and p23 increases the apparent affinity of Hsp90 for 5'-adenylyl-beta,gamma-imidodiphosphate and completely inhibits the ATPase activity
-
additional information
coiled-coil M-domains repress ClpB activity by encircling the AAA1 ring
-
additional information
-
cochaperone GmHop-1 may play a role in Hsp90 regulation
-
additional information
-
2 further inhibitors are found in a screen with 53440 compounds
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activator of Hsp90 ATPase
-
Aha1, 5fold activation of intrinsic ATPase activity
-
Apg2
-
at low concentration (0.0004 mM), Agp2 stimulates the ATPase activity of the enzyme
-
Bacillus subtilis ClpC adaptor protein MecA
-
the refolding activity of SyClpC is enhanced 3fold in presence of Bacillus subtilis ClpC adaptor protein MecA
-
EhAha1c
co-chaperone Aha1, i.e. activator of Hsp90 ATPase, lacking a canonical Aha1 N-terminal domain compared to other Aha1 co-chaperones. EhAha1c is capable of binding and stimulating ATPase activity of EhHsp90. The Aha1 protein is characterized by the presence of two domains joined by a small linker, interaction analysis with the enzyme, overview
-
GroES
-
required for the functioning of the Escherichia coli heat shock protein, also stimulates the reassembly
-
Hep1
-
Hsp70 escort protein, interacts with mtHsp70 and is crucial for maintaining native mtHsp70 in its functional state, Hep1 is required for the folding of the ATPase domain of mtHsp70. Folding of mtHsp70 is impaired in mitochondria lacking Hep1
-
ISCU
-
the iron-sulfur cluster scaffold protein, the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU, detailed interaction analysis
-
NRLLLTG
-
peptide binding to the substrate-binding site. Stimulates ATPase activity, eliminates stimulatory effect of geranylgeraniol
unfolded protein
-
reduced carboxymethylated alpha-lactalbumin, 0.08 mM, 28% stimulation above intrinsic activity
-
15-deoxyspergualin
-
stimulates the ATPase activity of mammalian and yeast cytosolic Hsc70 from 20 to 40%, no effect on HSC70 BiP and DnaJ-stimulated Hsc70 ATPase activity
15-deoxyspergualin
-
stimulates the ATPase activity of mammalian and yeast cytosolic Hsc70 from 20 to 40%, no effect on HSC70 BiP and DnaJ-stimulated Hsc70 ATPase activity
Asn-Asp-Leu-Leu-Leu-Thr-Gly
-
approx. 5fold activation of ATPase activity by NRLLLTG peptide
Asn-Asp-Leu-Leu-Leu-Thr-Gly
-
peptide NRLLLTG, 5fold and 2fold increase in ATPase activity at pH 7.0 and pH 9.0, respectively
ATP
-
ATP binding to nucleotide-binding domain 1 serves as a central regulatory switch for the chaperone, it triggers binding of polypeptides and stimulates ATP hydrolysis in the C-terminal nucleotide-binding domain 2 by more than 2 orders of magnitude
ATP
-
in 1:1 mixture with ATP-gammaS, greatly stimulates protein remodeling
ATP-gammaS
-
in 1:1 mixture with ATP, greatly stimulates protein remodeling
goniothalamin
-
a naturally occurring styryl-lactone, isolated from the air-dried bark of Goniothalamus tapis Miq., that increases both Km and kcat of Hsp90, it binds to the N-terminal domain of Hsp90 activates its ATPase activity, while inhibiting the chaperone function of Hsp90
goniothalamin
-
enhances the ATPase activity of the molecular chaperone Hsp90 (1.76fold at 0.04 mg/ml)
goniothalamin
-
a naturally occurring styryl-lactone, that increases both Km and kcat of Hsp90. Goniothalamin binds to the N-terminal domain of HtpG. Goniothalamin does not influence the interaction of HtpG with a non-native protein or the anti-aggregation activity of HtpG significantly. But it inhibits the activity of HtpG that assists refolding of a non-native protein in cooperation with the Hsp70 chaperone system. Domain competition in presence of goniothalamin, overview. The N-terminal domain inhibits the enhancement of the activity by goniothalamin, whereas HtpG lacking the N-terminal domain, i.e. the middle domain fused to the C-terminal domain, does not affect the enhancement
goniothalamin
-
enhances the ATPase activity of the molecular chaperone Hsp90 (1.56fold at 0.04 mg/ml)
GrpE
-
heat shock protein, cochaperonin, increases effectiveness of DnaK 40fold
-
Hsc20
-
the ATPase activity of mtHSP70 is accelerated by co-chaperone HSC20 and further accelerated by HSC20 plus scaffold protein ISCU. mtHSP70 binds preferentially to the D-state of ISCU and that HSC20 binds preferentially to the S-state of ISCU
-
kappa-casein
-
the enzyme exhibits a weak ATPase activity that is stimulated about 4fold by kappa-casein
-
kappa-casein
-
the enzyme exhibits a weak ATPase activity that is stimulated about 2fold by kappa-casein
-
poly-L-lysine
-
the enzyme exhibits a weak ATPase activity that is stimulated about 10fold by poly-L-lysine
poly-L-lysine
-
the enzyme exhibits a weak ATPase activity that is stimulated about 5fold by poly-L-lysine
additional information
-
aggregated glucose-6-phosphate dehydrogenase does not significantly affect the ATPase activity of the enzyme
-
additional information
-
aggregates of carboxymethylated alpha-lactalbumin, fluorescein-CALLQSRLLLSAPRRAAATAR, NRLLLTG, and tryptic fragments of casein smaller than 10 kDa fail to stimulate the DnaK-ClpB complex activity
-
additional information
mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. ClpB activation requires two signals: (1) interaction with the Hsp70 partner chaperone and (2) binding to substrate protein
-
additional information
-
aggregated glucose-6-phosphate dehydrogenase does not significantly affect the ATPase activity of the enzyme
-
additional information
deletion of the N-terminal domain activates the basal activity 2fold, whereas elimination of the M domain increases the ATPase activity 10fold in the presence of casein
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.118
ATP
-
Hsp82p, in the presence of Aha1p, at pH 7.2, temperature not specified in the publication
0.133
ATP
-
Hsp82p, at pH 7.2, temperature not specified in the publication
0.4325
ATP
recombinant enzyme, pH 7.4, temperature not specified in the publication
0.466
ATP
-
Hsp82p, in the presence of Hch1p, at pH 7.2, temperature not specified in the publication
0.66
ATP
-
in the presence of 0.04 mg/ml goniothalamin, at pH 8.0 and 37°C
0.73
ATP
-
in the presence of 0.04 mg/ml goniothalamin, at pH 8.0 and 37°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
cooperative mode of ATP hydrolysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00018
ATP
recombinant enzyme, pH 7.4, temperature not specified in the publication
0.0125
ATP
-
pH 7.4, 37°C, presence of 0.00048 mM DnaJ and 0.0009 mM GrpE proteins
0.0157
ATP
-
pH 7.4, 37°C, presence of 0.00097 mM DnaJ and 0.00091 mM GrpE proteins
0.0195
ATP
-
pH 8.0, 37°C in absence of goniothalamin at 0.04 mg/ml
0.0408
ATP
-
in the presence of 0.04 mg/ml goniothalamin, at pH 8.0 and 37°C
0.0438
ATP
-
pH 8.0, 37°C in presence of goniothalamin at 0.04 mg/ml
0.0438
ATP
-
in the presence of 0.04 mg/ml goniothalamin, at pH 8.0 and 37°C
0.167
ATP
-
pH 7.4, 37°C, presence of 0.00097 mM DnaJ and 0.0018 mM GrpE proteins
additional information
additional information
-
kcat for ATP approx. 0.0008, 0.0025 and 0.002 at pH 4.5, pH 7.0 and pH 9.0, respectively, in the presence of peptide NRLLLTG
-
additional information
additional information
-
ATPase activities are stimulated by unfolded carboxy-methyl lactalbumin and the hydrophobic peptide A7 (stimulation factor 1.2-3.9)
-
additional information
additional information
-
ATPase activity is enhanced by co-chaperones DnaJ and GrpE, more than 12fold stimulation is observed in the presence of each of these co-chaperones
-
additional information
additional information
ATPase activity is not stimulated by co-chaperones DnaJ and GrpE
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
ATP
recombinant enzyme, pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
3-[(E)-[2-[(2-amino-6-methylpyrimidin-4-yl)ethynyl]benzylidene]amino]-1,3-oxazolidin-2-one
-
pH and temperature not specified in the publication
additional information
additional information
inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
2,5-dichloro-N-[4-hydroxy-3-(2-hydroxynaphthalen-1-yl)phenyl]benzenesulfonamide
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.00009
2-fluoro-8-[(6-iodo-1,3-benzodioxol-5-yl)methyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00074
4-chloro-6-(4-[4-[4-(methylsulfonyl)benzyl]piperazin-1-yl]-1H-pyrazol-3-yl)benzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.001
4-chloro-6-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]benzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.0089
4-[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-1H-pyrazol-3-yl]-6-ethylbenzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.0006
4-[4-(4-benzylpiperazin-1-yl)-1H-pyrazol-3-yl]-6-chlorobenzene-1,3-diol
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.000028
5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)-1,2-oxazole-3-carboxamide
Saccharomyces cerevisiae
-
pH and temperature not specified in the publication
0.065 - 0.13
5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
0.0003
6-chloro-9-[(4-methoxy-3,5-dimethylpyridin-2-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
6-chloro-9-[(5-methoxy-4,6-dimethylpyridin-3-yl)methyl]-9H-purin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
8-(2-chloro-3,4,5-trimethoxybenzyl)-2-fluoro-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00028
8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9-(pent-4-yn-1-yl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
8-[(6-iodo-1,3-benzodioxol-5-yl)sulfanyl]-9-[3-(propan-2-ylamino)propyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-(cyclopropylamino)ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9-[2-[(2,2-dimethylpropyl)amino]ethyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.001 - 0.002
9-butyl-8-(3,4,5-trimethoxybenzyl)-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00018
9-butyl-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.00014
9-[3-(tert-butylamino)propyl]-8-[(2-iodo-5-methoxyphenyl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
diethyl (2-[6-amino-8-[(7-bromo[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro-1,3-benzothiazol-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
diethyl (2-[6-amino-8-[(7-chloro[1,3]thiazolo[4,5-c]pyridin-2-yl)sulfanyl]-9H-purin-9-yl]ethyl)phosphonate
Homo sapiens
-
pH and temperature not specified in the publication
0.000546
17-allylamino-17-demethoxygeldanamycin
Entamoeba histolytica
inhibition of cell growth, pH 7.4, temperature not specified in the publication
0.0309
17-allylamino-17-demethoxygeldanamycin
Entamoeba histolytica
inhibition of the ATPase activity, pH 7.4, temperature not specified in the publication
0.115
17-allylamino-17-demethoxygeldanamycin
Entamoeba histolytica
inhibition of the ATPase activity, in presence of co-chaperone EhAha1c, pH 7.4, temperature not specified in the publication
0.065
5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
Escherichia coli
-
pH 7.4, 37°C, presence of peptide NRLLLTG
0.13
5-[1-[(6-[5-[(benzyloxy)carbonyl]-4-biphenyl-4-yl-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoyl)(hexyl)amino]-2-[(1E)-butylideneamino]-2-oxoethyl]-2-(carboxymethoxy)benzoic acid
Escherichia coli
-
pH 7.4, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00283
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.006 mM HSC20
0.0075
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.015 mM ISCU
0.025
-
purified recombinant enzyme, pH 7.5, 25°C, in presence of 0.004 mM HSC20 and 0.015 mM ISCU
0.412
purified recombinant enzyme, pH 7.4, temperature not specified in the publication
additional information
additional information
-
high-throughput screening method in 96-well plates for ATPase activity of DnaK. Screening of potential inhibitors
additional information
-
mutation T213N or T612N produce a ca. 50% decrease in the ATPase activity, in mutant T213N/T612N the ATPase activity was approximately sevenfold lower than that of wild type ClpB, the ATPase of all ClpB variants is activated by soluble pseudosubstrates (casein and poly-lysine)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 45
-
approx. 12fold increase in reaction rate between 10°C and 15°C, approx. 4fold increase in reaction rate between 25°C and 35°C
25 - 70
-
approx. 64% of maximal activity at 40°C, approx. 50% of maximal activity at 65°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
210499, 210500, 210502, 210503, 210505, 210506, 210507, 210508, 210509, 210510, 210513, 210514, 210517, 210518, 654049, 654050, 654656, 656011, 657364, 667630, 667806, 668549, 669462, 696839, 697611, 700208, 701016, 701108, 701351, 734995, 755898
-
-
brenda
-
656160, 656262, 656348, 656552, 667113, 667512, 667964, 669876, 670011, 699538, 700208, 700375, 701351, 713375, 719075, 719344, 719653, 720049, 720801, 733348, 734233, 734536
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE