Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+/-)-aristeromycin + homocysteine
?
1-methyladenosine
?
-
-
-
-
r
2-aminoadenosine + homocysteine
?
-
-
-
-
r
2-aza-3-deazaadenosine + homocysteine
?
2-chloroadenosine + homocysteine
?
2-hydroxyadenosine + homocysteine
?
-
-
-
-
r
3-deaza-(+/-)-aristeromycin + homocysteine
?
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
4',5'-dehydroadenosine + H2O
adenosine
-
favors formation of 4',5'-dehydroadenosine, precursor reaction
-
r
7-deaza-8-azaadenosine + homocysteine
?
8-aminoadenosine + homocysteine
?
8-azaadenosine + homocysteine
?
adenosine N1-oxide + homocysteine
?
carboxylic analogue of adenosine
?
-
-
-
-
r
cysteine + adenosine
AdoCys
-
-
-
r
DL-homocysteine + 3-deazaadenosine
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine thiolactone
?
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine + H2O
S-adenosyl-L-homocysteine
-
-
-
r
N6-hydroxyadenosine + homocysteine
?
-
-
-
-
r
N6-methyladenosine + homocysteine
?
nebularine + homocysteine
?
pyrazomycin + homocysteine
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
tubercidin + L-homocysteine
?
-
-
-
-
r
additional information
?
-
(+/-)-aristeromycin + homocysteine
?
-
carbocyclic adenosine
-
-
r
(+/-)-aristeromycin + homocysteine
?
-
-
-
-
r
2-aza-3-deazaadenosine + homocysteine
?
-
-
-
-
r
2-aza-3-deazaadenosine + homocysteine
?
-
-
-
-
r
2-chloroadenosine + homocysteine
?
-
-
-
-
r
2-chloroadenosine + homocysteine
?
-
-
-
-
r
3-deaza-(+/-)-aristeromycin + homocysteine
?
-
carbocyclic 3-deazaadenosine
-
-
r
3-deaza-(+/-)-aristeromycin + homocysteine
?
-
-
-
-
r
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
-
-
-
-
r
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
-
-
-
r
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
-
-
-
-
r
3-deazaadenosine + L-homocysteine
3-deazaadenosylhomocysteine
-
-
-
?
7-deaza-8-azaadenosine + homocysteine
?
-
formycin A
-
-
r
7-deaza-8-azaadenosine + homocysteine
?
-
formycin A
-
-
r
7-deaza-8-azaadenosine + homocysteine
?
-
formycin A
-
-
r
7-deaza-8-azaadenosine + homocysteine
?
-
formycin A
-
-
r
7-deaza-8-azaadenosine + homocysteine
?
-
formycin A
-
-
r
8-aminoadenosine + homocysteine
?
-
-
-
-
r
8-aminoadenosine + homocysteine
?
-
-
-
-
r
8-azaadenosine + homocysteine
?
-
-
-
-
r
8-azaadenosine + homocysteine
?
-
-
-
-
r
adenosine N1-oxide + homocysteine
?
-
-
-
-
r
adenosine N1-oxide + homocysteine
?
-
-
-
-
r
adenosine N1-oxide + homocysteine
?
-
-
-
-
r
adenosine N1-oxide + homocysteine
?
-
-
-
-
r
adenosine N1-oxide + homocysteine
?
-
-
-
-
r
DL-homocysteine + 3-deazaadenosine
?
-
-
-
-
r
DL-homocysteine + 3-deazaadenosine
?
-
-
-
-
?
DL-homocysteine + 3-deazaadenosine
?
-
-
-
-
r
DL-homocysteine + 3-deazaadenosine
?
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
Micromonospora faeni
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
-
?
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
-
-
-
?
inosine + homocysteine
?
-
-
-
-
r
inosine + homocysteine
?
-
-
-
-
r
inosine + homocysteine
?
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
?
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
N6-methyladenosine + homocysteine
?
-
-
-
-
r
N6-methyladenosine + homocysteine
?
-
-
-
-
r
N6-methyladenosine + homocysteine
?
-
-
-
-
r
N6-methyladenosine + homocysteine
?
-
-
-
-
r
N6-methyladenosine + homocysteine
?
-
-
-
-
r
nebularine + homocysteine
?
-
-
-
-
r
nebularine + homocysteine
?
-
-
-
-
r
nebularine + homocysteine
?
-
-
-
-
r
nebularine + homocysteine
?
-
-
-
-
r
nebularine + homocysteine
?
-
-
-
-
r
pyrazomycin + homocysteine
?
-
-
-
-
r
pyrazomycin + homocysteine
?
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
the reversible catalysis depends on the binding of NAD+ to the enzyme
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Micromonospora faeni
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
through the hydrolysis of S-adenosyl-L-homocysteine, the SAH hydrolase prevents the accumulation of S-adenosyl-L-homocysteine that would otherwise lead to an inhibition of the S-adenosyl-L-methionine-dependent methylation reactions, including those that are required for the maturation (i.e. 5'-capping) of viral mRNAs
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
reversible hydrolysis, five-step process of SAH hydrolysis by SAHH
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
substrate binding site structure, overview
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
additional information
?
-
-
homology-dependent gene silencing gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
polymorphism has no effect on the total plasma homocysteine
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
using a yeast two-hybrid system it shown that AdoHcyase directly interacts with Streptococcal pyrogenic exotoxin B protease. Furthermore, it is shown that AdoHcyase gets cleaved and inactivated by Streptococcal pyrogenic exotoxin B protease, inducing hypermethioninemia
-
-
?
additional information
?
-
-
SAHH interacts with H19 lncRNA in ribonucleoprotein complexes, the SAHH-H19 interaction is specific
-
-
?
additional information
?
-
the enzyme binds the reaction intermediate analogues 3'-oxo-aristeromycin (3KA) and noraristeromycin (NRN), and reacts with 3KA in a Michael addition
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
enzyme adenosine binding structure, overview
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine + H2O
S-adenosyl-L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
additional information
?
-
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
L-homocysteine + adenosine
S-adenosyl-L-homocysteine + H2O
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
Micromonospora faeni
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
through the hydrolysis of S-adenosyl-L-homocysteine, the SAH hydrolase prevents the accumulation of S-adenosyl-L-homocysteine that would otherwise lead to an inhibition of the S-adenosyl-L-methionine-dependent methylation reactions, including those that are required for the maturation (i.e. 5'-capping) of viral mRNAs
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?, r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
r
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
-
-
-
?
additional information
?
-
-
homology-dependent gene silencing gene codes for an S-adenosyl-L-homocysteine hydrolase required for DNA methylation-dependent gene silencing
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
polymorphism has no effect on the total plasma homocysteine
-
-
?
additional information
?
-
-
enzyme redistributes in response to chemotactic signals
-
-
?
additional information
?
-
-
using a yeast two-hybrid system it shown that AdoHcyase directly interacts with Streptococcal pyrogenic exotoxin B protease. Furthermore, it is shown that AdoHcyase gets cleaved and inactivated by Streptococcal pyrogenic exotoxin B protease, inducing hypermethioninemia
-
-
?
additional information
?
-
-
SAHH interacts with H19 lncRNA in ribonucleoprotein complexes, the SAHH-H19 interaction is specific
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase associates with diamine oxidase as part of a larger multienzyme complex that may function in planta as a nicotine metabolic channel
-
-
?
additional information
?
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
additional information
?
-
-
S-adenosyl-L-homocysteine hydrolase is the key enzyme of methylation metabolism. SAH1 expression is coordinately regulated by genes involved in phospholipid biosynthesis. Sah1p depletion leads to significant changes in lipid metabolism, resulting in accumulation of triglycerides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+
-
-
NAD+
-
essential for adenosine binding
NAD+
-
contains 0.27 mol of NAD+ per mol of subunit
NAD+
-
contains 0.65 mol of NAD+ per mol of subunit
NAD+
-
enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Final affinity of enzyme for NAD+ is about micromolar. Slow binding exhibits saturation kinetics with a rate constant of 0.006 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
NAD+
-
enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Slow binding exhibits saturation kinetics with a rate constant of 0.06 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme
NAD+
-
inactivation by (E)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine results in 66% loss of NAD+, by (Z)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine in 27% loss, and by (E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine in 28% loss, respectively
NAD+
presence of Cu2+ results in release of NAD+ cofactors
NAD+
-
the enzyme contains four molecules of tightly-bound NAD+ per tetramer of which about 40% is in the reduced form
NAD+
wild-type, 3.5 mol per mol of tetramer, mutant Y143C, 3.1 mol per mol of tetramer, mutant E115L, 4.6 mol per mol of tetramer
NAD+
-
wild-type, about 81% of cofactor bound as NAD+, mutant A89V, about 70.5% of cofactor bound as NAD+
NAD+
-
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme
NAD+
comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme. Y430 in the C-terminal extension of human SAHH may slightly influence binding of NAD+ and NADH to apo-SAHH
NAD+
mode of binding and oxidation state, overview
NAD+
NAD+ binding mode, overview. Two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH, which is important in NAD+ binding, and thus exposes the bound cofactor to the solvent. The difference explains the higher NAD+ requirement of tmSAHH because of the reduced affinity. Binding pocket structure, overview
NAD+
the enzyme tetramer tightly but not covalently binds an NAD+ cofactor, binding structure, overview. The cofactor-binding domain comprises residues 197-351. The basic element of the secondary structure in this domain is a six-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. The six-stranded parallel beta-sheet is flanked by four alpha-helices and constitutes a characteristic dinucleotide-binding motif or Rossmann fold composed of two betaalphabetaalphabeta units
NAD+
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NAD+
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic origin is presented, with an emphasis on the two principal domains of SAHase subunit based on the Rossmann motif. The first domain is involved in the binding of a substrate, e.g., S-adenosyl-L-homocysteine or adenosine and the second domain binds the NAD+ cofactor. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
NADH
-
contains 0.19 mol of NAD+ per mol of subunit
NADH
-
contains 0.47 mol of NAD+ per mol of subunit
NADH
-
wild-type, about 81% of cofactor bound as NAD+, mutant A89V, about 70.5% of cofactor bound as NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-5'-noraristeromycin
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
(1R,2S,3R)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
CAS:1214735-71-3
(1R,2S,3R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopentane-1,2-diol
-
-
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
-
-
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
-
-
(1R,2S,3S)-3-(8-aminoimidazo[1,2-a]pyrazin-3-yl)cyclopentane-1,2-diol
-
-
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(6-amino-2-fluoro-9H-purin-9-yl)cyclopentane-1,2-diol
-
-
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
-
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
-
-
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
-
-
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
-
-
(1S,2R,5R)-5-(6-amino-9H-purin-9-yl)-3-(prop-1-yn-1-yl)cyclopent-3-ene-1,2-diol
-
i.e. prop-1-yn-1-yl-substitued neplanocin A, 81% inhibition at 0.01 mM
(1S,2R,5R)-5-(6-amino-9H-purin-9-yl)-3-phenylcyclopent-3-ene-1,2-diol
-
i.e. phenyl-substitutued neplanoocin A, 64% inhibition at 0.1 mM
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
-
-
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
-
-
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
-
-
(2E)-3-(4-chlorophenyl)prop-2-enoic acid
-
(2E)-3-(4-methoxyphenyl)prop-2-enoic acid
-
(2R)-3-(adenin-9-yl)-2-hydroxypropanoic acid
-
-
(2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
in rats fed by the enzyme inhibitor, the total plasma cholesterol and phospholipids decreases
(2R,3R)-4-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)-2,3-dihydroxy-N-methylbutanamide
-
(2R,3R)-methyl 4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
-
(2R,3R)-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid
in rats fed by the enzyme inhibitor, the total plasma cholesterol and phospholipids decreases
(2R,3R)-N-methyl-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanamide
-
(2S)-3-(adenin-9-yl)-2-hydroxypropanoic acid
-
-
(6'R)-6'-C-methylneplanocin A
(E)-4',5'-didehydro-2',5'-dideoxy-5'-fluoroadenosine
-
-
(E)-4',5'-didehydro-5'-deoxy-5'-chloro-5'-fluoroadenosine
-
competitive
(E)-5'-deoxy-5'-(iodomethylene)adenosine
-
similar inhibitory activity against both Trichosoma vaginalis and trypanosomes, inhibits growth of Trichosoma vaginalis strain T1
(E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 28% loss of NAD+
(E)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, type I inhibitor. Inactivation results in 66% loss of NAD+
(E)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
(E)-9-(5-deoxy-5-fluoro-beta-D-threo-pent-4-enofuranosyl)-9H-purin-6-amine
-
competitive
(S)-9-(2,3-Dihydroxypropyl)adenine
100 nM, 7% loss of activity
(Z)-4',5'-didehydro-2',5'-dideoxy-5'-fluoroadenosine
-
competitive
(Z)-4',5'-didehydro-5'-chloro-5'-deoxyadenosine
-
competitive
(Z)-4',5'-didehydro-5'-deoxy-5'-chloro-5'-fluoroadenosine
-
competitive
(Z)-5'-deoxy-5'-(iodomethylene)adenosine
-
similar inhibitory activity against both Trichosoma vaginalis and trypanosomes, inhibits growth of Trichosoma vaginalis strain T1
(Z)-5'-fluoro-4',5'-didehydro-5'-deoxyadenosine
-
MDL-28842
(Z)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 27% loss of NAD+
(Z)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
(Z)-9-(5-deoxy-5-fluoro-beta-D-threo-pent-4-enofuranosyl)-9H-purin-6-amine
-
competitive
1,2,4,triazole-3-carboxamide riboside
-
ribavirin
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
1-(bromomethyl)-2,4-difluorobenzene
-
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
2'3'-dideoxyadenosine
-
-
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
4.56% inhibition at 0.0025 mM; 8.23% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)-amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
4.89% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
30.19% inhibition at 0.0025 mM
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
27.15% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
85.72% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
86.56% inhibition at 0.0025 mM
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
19.23% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(diethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
20.16% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(ethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
79.46% inhibition at 0.0025 mM
2-((4-(1H-pyrrol-1-yl)phenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
21.46% inhibition at 0.0025 mM
2-((4-fluorophenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)-amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
-
2.63% inhibition at 0.0025 mM
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl]amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-amino-4'-alpha-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
2-chloro-3-deazaadenosine
-
irreversible
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(2-nitrobenzene-1-sulfonyl)piperazin-1-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[(2-fluorophenyl)methyl]amino]-2-oxoethyl)amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
3-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-(6-amino-9H-purin-9-yl)cyclopentane-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-acetylpyridine adenine dinucleotide
-
0.02 mM, 94% residual activity in presence of 0.05 mM NAD, pH 7.4
3-deaza-(+/-)-aristeromycin
3-deaza-adenosine
-
the inhibitor of S-adenosyl homocysteine hydrolase prevents oxidative damage and cognitive impairment following folate and vitamin E deprivation in a murine model of age-related, oxidative stress-induced neurodegeneration. The inhibitor might by useful in therapeutic approach to delay neurodegeneration in Alzheimer's disease
3-deazaadenosylhomocysteine
-
-
3-deazaaristeromycylhomocysteine
-
-
3-deazaneplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
3-pyridinaldehyde adenine dinucleotide
-
0.02 mM, 77% residual activity in presence of 0.05 mM NAD, pH 7.4
4',5'-dehydroadenosine
-
-
4'-beta-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
4-(3-hydroxyprop-1-en-1-yl)-2-methoxyphenol
coniferyl alcohol, molecular docking studies show that coniferyl alcohol is well docked into the active cavity of SAHH. Several H-bonds are formed between them, which stabilize coniferyl alcohol in the active site of rSAHH with a proper conformation
4-chloro-1,3-dihydroxyphenol
-
4-chlorobenzene-1-carboperoxoic acid
-
4-methoxybenzaldehyde
i.e. anisaldehyde
4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
-
5'-deoxy,5'-methylthioadenosine
-
-
5'-deoxy-5',5'-difluoradenosine
5'-iodo-5'-deoxyadenosine
-
-
5'-S-cyano-5'-thioadenosine
-
5'-S-ethynyl-5'-thioadenosine
-
5'-S-vinyl-5'-thioadenosine
-
5,5'-dithiobis-(2-nitrobenzoate)
-
-
5-(4-amino-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
5-(6-amino-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
5-(6-aminopurin-9-yl)-3-hydroxymethylcyclopent-3-ene-1,2-diol
-
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
i.e. fluoroneplanocin A, mechanism-based inhibitor, crystallization data
5-(6-aminopurin-9-yl)-4-fluorocyclopent-3-ene-1,2-diol
-
5-(6-aminopurin-9-yl)-cyclopent-3-ene-1,2-diol
-
5-amino-4-imidazole carboxamide riboside
-
-
6'-beta-fluoroaristeromycin
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
8-(3-aminopropylamino)adenosine
-
-
9-(2,3-Dihydroxypropyl)adenine
-
-
9-(2-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine
-
-
9-(2-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine oxime
-
(E/Z)
9-(3-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine
-
-
9-(3-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine oxime
-
(E/Z)
9-(5,6-dideoxy-6-iodo-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-iodohomoadenosine, strong
9-(6-bromo-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-bromohomoadenosine, partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
9-(alpha-L-lyxo-pentodialdo-1,4-furanosyl)adenine
-
-
9-(alpha-L-lyxo-pentodialdo-1,4-furanosyl)adenine oxime
-
(E/Z)
9-(beta-D-arabino-pentodialdo-1,4-furanosyl)adenine
-
-
9-(beta-D-arabino-pentodialdo-1,4-furanosyl)adenine oxime
-
(E/Z)
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine
-
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine (adenosine-5'-carboxaldehyde)
-
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-benzyloxime
-
(E/Z)
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-ethyloxime
-
(E/Z)
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-methyloxime
-
(E/Z)
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine oxime
-
(E/Z)
9-(S)-(2,3-dihydroxypropyl)-adenine
-
inhibitor of SAH-hydrolase. Application on tobacco seeds during 6 days during the germination period. The transient drug treatment induces dosage-dependent global DNA hypomethylation mitotically transmitted to adult plants, pleiotropic developmental defects including decreased apical dominance, altered leaf and flower symmetry, flower whorl malformations and reduced fertility, and dramatic upregulation of floral organ identity genes NTDEF, NTGLO and NAG1 in leaves
9-beta-D-arabinofuranosyl-2-chloroadenine
-
irreversible
9-beta-D-arabinofuranosyl-2-fluoroadenine
-
irreversible
9-beta-D-arabinofuranosyl-3-deazaadenine
-
irreversible
9-beta-D-arabinofuranosyladenine
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
9-[(1'R,2'S,3'S,4'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-adenine
-
-
9-[5,6,7,8-tetradeoxy-8-iodo-beta-D-ribo-oct-5(E)-en-7-yno-furanosyl]adenine
-
-
9-[5,6,7,8-tetradeoxy-beta-D-ribo-oct-5(E)-en-7-ynofuranosyl]adenine
-
-
9H-purin-6-amine, 9-(6-chloro-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-chlorohomoadenosine partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
acid ammonium sulfate
-
-
adenine-arabinoside
100 nM, 10% loss of activity
adenosine 5'-carboxylate
-
competitive
adenosine dialdehyde
irreversible inhibitor
Adenosine diphosphate
-
-
adenosine-2',3'-dialdehyde
-
inhibition of the enzyme, mimicks the induction of caspase-like activity and DNA fragmentation induced by adenosine
adenosine-2'-monophosphate
-
-
adenosine-3',5'-cyclic monophosphate
-
-
Adenosine-3'-monophosphate
-
-
adenosine-5'-monophosphate
adenosylornithine
-
sinefungin
ADP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
AMP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
arabinosylhypoxanthine
-
-
beta-thionicotinamide adenine dinucleotide
beta-thionicotinamide adenine dinucleotide, reduced form
CaCl2
-
reduces adenosine binding
carbocyclic 3-deazaadenosine
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
cis-diaminedichloride platinum
Cu2+
noncompetitive, binding of Cu2+ results in release of NAD+ cofactors. Cu2+ binds at the central channel and interrupts subunit interactions
dihydroxypropyladenine
-
DHPA
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]propanoate
63.62% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
79.87% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(6-amino-9H-purin-9-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
57.21% inhibition at 0.2 mM
ethyl 3-[(2R,3R,4R,5S)-5-[2-(acetylamino)-6-[(diphenylcarbamoyl)oxy]-9H-purin-9-yl]-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
87.58% inhibition at 0.2 mM
ethyl 3-[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)amino]-4-hydroxytetrahydrofuran-2-yl]propanoate
81.13% inhibition at 0.2 mM
H19 lncRNA
-
the developmentally regulated H19 lncRNA binds to enzyme S-adenosylhomocysteine hydrolase (SAHH) and inhibits its function both in vivo and in vitro. Binding to U-rich elements of H19 inhibits SAHH activity in vitro. The interaction prevents SAHH from hydrolysing SAH that blocks DNA methylation by DNMT3B at numerous genomic loci. The SAHH-H19 interaction is specific
-
Isothiocyanate
-
fluorescent isothiocyanate
methyl (2E)-3-[4-(bromomethyl)phenyl]prop-2-enoate
-
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
-
-
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
-
-
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
-
N-(isoindolin-2-yl)-N-methyl-2-((1-methyl-1H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-acetamide
-
54.24% inhibition at 0.0025 mM
N-(isoindolin-2-yl)-N-methyl-2-((2-methyl-2H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl) ethyl)amino)ethyl)amino)-acetamide
-
38.24% inhibition at 0.0025 mM
N-(isoindolin-2-yl)-N-methyl-2-((2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)(4-tolyl)amino)acetamide
-
6.97% inhibition at 0.0025 mM
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
N2-[2-[(1-acetylpiperidin-4-yl)(methyl)amino]-2-oxoethyl]-N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[2,3-dihydro-1H-inden-2-yl(ethyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(piperidin-4-yl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(trans-4-phenylcyclohexyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
inhibitor compound crystal structure determination and analysis, overview. The single crystal X-ray structure of 14n shows an intramolecular eight-membered ring hydrogen bond interaction
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(ethylamino)ethyl]glycinamide hydrochloride
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-piperidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(3-pyrrolidin-1-ylpropyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-methyl(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(dimethylamino)ethyl]glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroquinolin-1(2H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methy-(phenyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl(1,2,3,4-tetrahydronaphtalen-2-yl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[1-(methylsulfonyl)piperidin-4-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[4-(methylsulfonyl)piperadin-1-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[1-(methoxycarbonyl)piperidin-4-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[4-(methoxycarbonyl)piperidin-1-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
-
-
Na+
-
reduces adenosine binding
nicotinamide 1,N6-ethenoadenine dinucleotide
-
0.02 mM, 95% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinamide guanine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinamide hypoxanthine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
nicotinic acid adenine dinucleotide
-
0.02 mM, 96% residual activity in presence of 0.05 mM NAD, pH 7.4
Nucleocidin
-
irreversible
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Rb+
activates, but is also a noncompetitive inhibitor
reduced 3-acetylpyridine adenine dinucleotide
-
0.02 mM, 52% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced 3-pyridinaldehyde adenine dinucleotide
-
0.02 mM, 9% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced nicotinamide hypoxanthine dinucleotide
-
0.02 mM, 98% residual activity in presence of 0.05 mM NAD, pH 7.4
reduced thionicotinamide adenine dinucleotide
-
0.02 mM, 8% residual activity in presence of 0.05 mM NAD, pH 7.4
S-adenosyl-L-homocysteine
tert-butyl (2R)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl (2S)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl 2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
-
-
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
-
-
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]ethylcarbamate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]methylcarbamate
-
-
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]propan-2-ylcarbamate
-
-
tetraethylene pentamine
-
65% inhibition at 0.0001 mM, 80% inhibition at 0.001 mM
Thionicotinamide adenine dinucleotide
-
0.02 mM, 74% residual activity in presence of 0.05 mM NAD, pH 7.4
trans-diaminedichloride platinum
Zn2+
enzyme binding structure, potent noncompetitive inhibition, isothermal titration calorimetry, overview. A tetrahedral zinc binding site, formed by three highly conserved amino acid residues involving S (Cys85), N (His323), and two O (Asp139) ligand atoms, is located in the active site, where, together with the H323-F324 molecular gate, the divalent cation shuts access to the active site of the enzyme
(+/-)-aristeromycin
-
carbocyclic adenosine; competitive
(+/-)-aristeromycin
-
competitive
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
-
-
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
-
-
-
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
-
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
-
-
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
-
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
-
-
(6'R)-6'-C-methylneplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
(6'R)-6'-C-methylneplanocin A
-
-
(E)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
-
-
(E)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
-
-
(Z)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
-
-
(Z)-9-(5-deoxy-5-fluoro-beta-D-erythro-pent-4-enofuranosyl)adenine
-
-
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
-
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
-
-
2'-deoxyadenosine
-
-
2'-deoxyadenosine
-
irreversible
2'-deoxyadenosine
-
reversible
2'-deoxyadenosine
time course of PaSAHase inactivation by 2'-deoxyadenosine, influence of K+ and Rb+ ions, overview
2-aminoaristeromycin
-
20fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-aminoaristeromycin
-
20fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-aza-3-deazaadenosine
-
competitive
2-aza-3-deazaadenosine
-
competitive
2-chloroadenosine
-
-
2-chloroadenosine
-
irreversible
2-fluoroaristeromycin
-
24fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-fluoroaristeromycin
-
24fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-fluoronoraristeromycin
-
-
2-fluoronoraristeromycin
-
3-deaza-(+/-)-aristeromycin
-
-
3-deaza-(+/-)-aristeromycin
-
carbocyclic 3-deazaadenosine; competitive
3-deaza-(+/-)-aristeromycin
-
-
3-deaza-(+/-)-aristeromycin
-
-
3-deazaadenosine
-
-
3-deazaadenosine
-
competitive
3-deazaadenosine
-
competitive
3-deazaadenosine
-
35.37% inhibition at 0.0025 mM
5'-deoxy-5',5'-difluoradenosine
-
-
5'-deoxy-5',5'-difluoradenosine
-
-
7-deaza-8-azaadenosine
-
formycin A
7-deaza-8-azaadenosine
-
competitive; formycin A
7-deaza-8-azaadenosine
-
competitive; formycin A
8-Aminoadenosine
-
competitive
8-Aminoadenosine
-
competitive
8-azaadenosine
-
competitive
8-azaadenosine
-
competitive
9-beta-D-arabinofuranosyladenine
-
irreversible
9-beta-D-arabinofuranosyladenine
-
-
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
-
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
adenine
-
-
adenosine
-
-
adenosine
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
adenosine N1-oxide
-
-
adenosine N1-oxide
-
competitive
adenosine N1-oxide
-
competitive
adenosine-5'-monophosphate
-
-
adenosine-5'-monophosphate
-
-
adenosine-5'-monophosphate
-
poor
adenosine-5'-monophosphate
-
-
adenosine-5'-monophosphate
-
-
arabinosyladenine
-
-
aristeromycin
-
98.35% inhibition at 0.0025 mM
ATP
-
-
ATP
-
adenosine analogs exhibit the following trend in the half-maximal inhibitory concentrations: adenosine > AMP > ADP = ATP
beta-thionicotinamide adenine dinucleotide
-
binding affinity 40 nM, 30% loss of activity after 12 h
beta-thionicotinamide adenine dinucleotide
-
binding affinity 0.0006-0.015 mM, 60% loss of activity after 30 min
beta-thionicotinamide adenine dinucleotide, reduced form
-
binding affinity 40 nM, 30% loss of activity after 12 h
beta-thionicotinamide adenine dinucleotide, reduced form
-
binding affinity 0.0006-0.015 mM, 100% loss of activity after 30 min
cAMP
-
-
cis-diaminedichloride platinum
-
-
cis-diaminedichloride platinum
-
-
D-eritadenine
100 nM, 30% loss of activity
D-eritadenine
potent inhibitor
dithiothreitol
-
together with adenosine
dithiothreitol
0.8 M, reduces activity
DL-homocysteine
-
-
DL-homocysteine
-
competitive
DZ2002
reversible inhibitor
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
-
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
-
-
Inosine
-
-
KCl
-
with ATP-Mg acetate
KCl
-
with ATP-Mg acetate
L-homocysteine
-
-
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002, potent reversible type III inhibitor, blocks S-adenosylhomocysteine hydrolase more effectively than type I inhibitor, but cytotoxicity is greatly reduced
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002, potent reversible type III inhibitor, blocks S-adenosylhomocysteine hydrolase more effectively than type I inhibitor, but cytotoxicity is greatly reduced
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002. The inhibitor suppresses antigen-induced specific immune responses, particularly type 1 helper T cell responses through inhibition of S-adenosyl-L-homocysteine hydrolase and elevation of endogenous S-adenosyl-L-homocysteine
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
-
-
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
-
-
-
N6-methyladenosine
-
-
N6-methyladenosine
-
competitive
N6-methyladenosine
-
competitive
nebularine
-
-
neplanocin A
-
-
neplanocin A
-
IC50: 47 nM
neplanocin A
strong inhibition, oxidation upon binding to form the complex enzyme/NADH/3'-keto-neplanocin
neplanocin A
NepA, a natural product that is cytotoxic upon long term exposure and shows adenosine deaminase and adenosine kinase activity
neplanocin A
-
potent antiviral based on the inhibitory effect on the replication of two reporter viruses, vesicular stomatitis virus and vaccinia virus
neplanocin A
-
IC50: 101 nM
noraristeromycin
-
-
Pyrazomycin
-
competitive
Pyrazomycin
-
competitive
ribavirin
-
binds to adenosine-binding site of enzyme and reduces the NAD+ cofactor to NADH. Selective for trypanosomal enzyme over human enzyme, as the slow inactivation step is 5fold faster with the trypanosomal enzyme
ribavirin
-
binds to adenosine-binding site of enzyme and reduces the NAD+ cofactor to NADH. Selective for trypanosomal enzyme over human enzyme, as the slow inactivation step is 5fold faster with the trypanosomal enzyme
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
competitive
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
-
trans-diaminedichloride platinum
-
-
trans-diaminedichloride platinum
-
-
tubercidin
-
-
tubercidin
-
inhibition of enzyme as well as of chemotaxis and chemotaxis-dependent cell streaming
tubercidin
-
inhibition of enzyme as well as of chemotaxis, at concentrations that have little effect on cell viability
additional information
-
not inhibitory: azido-cAMP
-
additional information
L-adenosine and L-adenosine-5'-carboxaldehyde oximes are inactive as inhibitors
-
additional information
-
less than 4% inhibition at 0.02 mM, in presence of 0.05 mM NAD, pH 7.4: thionicotinamide adenine dinucleotide, 3-pyridinaldehyde adenine dinucleotide, 3-acetylpyridine adenine dinucleotide, nicotinic acid adenine dinucleotide, nicotinamide hypoxanthine dinucleotide, nicotinamide guanine dinucleotide, nicotinamide 1,N6-ethenoadenine dinucleotide, reduced thionicotinamide adenine dinucleotide, reduced 3-pyridinaldehyde adenine dinucleotide, reduced 3-acetylpyridine adenine dinucleotide, reduced nicotinamide hypoxanthine dinucleotide
-
additional information
-
inactive: 4-amino-1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidin-2(1H)-one
-
additional information
-
optimization of a series of S-adenosyl-L-homocysteine hydrolase (AdoHcyase) inhibitors based on non-adenosine analogues leads to very potent compounds
-
additional information
molecular docking study and simulations
-
additional information
-
molecular docking study and simulations
-
additional information
pentanediamide derivatives were designed, synthesized and evaluated as S-adenosyl-L-homocysteine hydrolase inhibitors
-
additional information
structure of the monovalent cation binding site, overview. The major structural difference between the closed/semi-open and open states concerns the conformation of Q65 (PaSAHase numbering). In the open state this residue is located far away from the metal binding loop and its side chain is disordered in at least two conformations
-
additional information
-
structure of the monovalent cation binding site, overview. The major structural difference between the closed/semi-open and open states concerns the conformation of Q65 (PaSAHase numbering). In the open state this residue is located far away from the metal binding loop and its side chain is disordered in at least two conformations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00004
(1R,2S,3R)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000055
(1R,2S,3R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000303
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000455
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
(1R,2S,3S)-3-(8-aminoimidazo[1,2-a]pyrazin-3-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.001223
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.003644
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.004827
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000016
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000041
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000236
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.002124
(1R,2S,4r)-4-(6-amino-2-fluoro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
13 - 16
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
-
0.61 - 0.85
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
-
2.1 - 7.5
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
-
0.000024
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
Homo sapiens
-
pH and temperature not specified in the publication
0.000195
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.004125
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000976
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.00969
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000269
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
Homo sapiens
-
pH and temperature not specified in the publication
0.000571
(2E)-3-(4-chlorophenyl)prop-2-enoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000986
(2E)-3-(4-methoxyphenyl)prop-2-enoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.1
(6'R)-6'-C-methylneplanocin A
Plasmodium falciparum
-
pH and temperature not specified in the publication
0.06
(E)-5'-deoxy-5'-(iodomethylene)adenosine
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.076
(Z)-5'-deoxy-5'-(iodomethylene)adenosine
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
24 - 47.2
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
-
0.000913
1-(bromomethyl)-2,4-difluorobenzene
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.00853
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
-
37°C
0.001245
1H-benzotriazol-1-ol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.07882 - 0.5
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
0.214
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)-amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00761
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.02534
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)-(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00048
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(1-methyl-1H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00044
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(2-methyl-2H-indazol-5-yl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.0156
2-((2-((2-(ethylamino)ethyl)amino)-2-oxoethyl)(4-tolyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.01408
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(diethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00073
2-((4-(1H-pyrrol-1-yl)phenyl)(2-((2-(ethylamino)-ethyl)amino)-2-oxoethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.01212
2-((4-(1H-pyrrol-1-yl)phenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.5
2-((4-fluorophenyl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)-amino)ethyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
IC50 above 0.5 mM, at pH 8.0 and 37°C
0.00015
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.01136
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl]amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.01136
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00451 - 0.0907
2-aminoaristeromycin
0.00198 - 0.0472
2-fluoroaristeromycin
0.0006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00011
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00032
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000052
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0002
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
0.000081
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.00053
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0027
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00023
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00033
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00878
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[(2-fluorophenyl)methyl]amino]-2-oxoethyl)amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00007
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.017
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
0.0012
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0015
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00878
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.000005
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00552
3-deazaadenosine
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00111
4-chloro-1,3-dihydroxyphenol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000565
4-chlorobenzene-1-carboperoxoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000679
4-fluorobenzoic acid
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000899
4-methoxyaniline
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.002131
4-methoxybenzaldehyde
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000034
4-[(1E)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.00087
5-(6-aminopurin-9-yl)-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.00048
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.00767
5-(6-aminopurin-9-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.00583
5-(6-aminopurin-9-yl)-cyclopent-3-ene-1,2-diol
Homo sapiens
pH 7.2, 37°C
0.0042
adenosine
Oryctolagus cuniculus
-
37°C, pH 7.2
0.04
adenosine-5'-oxime
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.36
AMP
Oryctolagus cuniculus
-
37°C, pH 7.2
0.00049 - 0.01
aristeromycin
0.018
Chloroquine
Plasmodium falciparum
-
pH and temperature not specified in the publication
4.51 - 20
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
-
0.144
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.0796
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.171
ethyl 3-[(2R,3R,4R,5S)-4-(acetyloxy)-5-(6-amino-9H-purin-9-yl)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.00043
ethyl 3-[(2R,3R,4R,5S)-5-[2-(acetylamino)-6-[(diphenylcarbamoyl)oxy]-9H-purin-9-yl]-4-(acetyloxy)-3-[(tert-butoxycarbonyl)(methyl)amino]tetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.0954
ethyl 3-[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-3-[(tert-butoxycarbonyl)amino]-4-hydroxytetrahydrofuran-2-yl]propanoate
Leishmania donovani
at pH 7.2 and 37°C
0.001399
ethyl 4-aminobenzoate
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000814
methyl (2E)-3-[4-(bromomethyl)phenyl]prop-2-enoate
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000044
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
Homo sapiens
-
at pH 7.2 and 37°C
0.00089
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
Homo sapiens
-
at pH 7.2 and 37°C
0.00072
metronidazole
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
0.0046
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
3.3 - 18
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
-
0.00203
N-(isoindolin-2-yl)-N-methyl-2-((1-methyl-1H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)amino)-acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00413
N-(isoindolin-2-yl)-N-methyl-2-((2-methyl-2H-indazol-5-yl)(2-oxo-2-((2-(piperidin-1-yl) ethyl)amino)ethyl)amino)-acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.1019
N-(isoindolin-2-yl)-N-methyl-2-((2-oxo-2-((2-(piperidin-1-yl)ethyl)amino)ethyl)(4-tolyl)amino)acetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
0.0046
N2-[2-[(1-acetylpiperidin-4-yl)(methyl)amino]-2-oxoethyl]-N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00064
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[2,3-dihydro-1H-inden-2-yl(ethyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(piperidin-4-yl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.00053
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-(2-[methyl(trans-4-phenylcyclohexyl)amino]-2-oxoethyl)-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.000013
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0000085
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(ethylamino)ethyl]glycinamide hydrochloride
Homo sapiens
-
pH 7.2, 37°C
0.000005
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride
Homo sapiens
-
pH 7.2, 37°C
0.00032
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-piperidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000052
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00033
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-(3-pyrrolidin-1-ylpropyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.1
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-methyl(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
above, pH 7.2, 37°C
0.00013
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[2,3-dihydro-1H-inden-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(dimethylamino)ethyl]glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0002
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl(methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.017
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroisoquinolin-2(1H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0023
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[3,4-dihydroquinolin-1(2H)-yl]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.0027
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methy-(phenyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000081
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl(1,2,3,4-tetrahydronaphtalen-2-yl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00023
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[1-(methylsulfonyl)piperidin-4-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000049
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[methyl-[4-(methylsulfonyl)piperadin-1-yl]amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.00089
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[1-(methoxycarbonyl)piperidin-4-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.000044
N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[[4-(methoxycarbonyl)piperidin-1-yl](methyl)amino]-2-oxoethyl]-N1-(2-pyrrolidin-1-ylethyl)glycinamide
Homo sapiens
-
pH 7.2, 37°C
0.2
neoplanocin A
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.0000015 - 0.000101
neplanocin A
1.1 - 3.1
noraristeromycin
0.0006
tert-butyl (2R)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00011
tert-butyl (2S)-2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00015
tert-butyl 2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.0012
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]piperidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.0015
tert-butyl 3-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]pyrrolidine-1-carboxylate
Homo sapiens
-
pH 7.2, 37°C
0.00006
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]ethylcarbamate
Homo sapiens
-
pH 7.2, 37°C
0.00007
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]methylcarbamate
Homo sapiens
-
pH 7.2, 37°C
0.000049
tert-butyl [2-[2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-[(2,3-dihydro-1H-inden-2-yl)(methyl)amino]-2-oxoethyl]amino)acetamido]ethyl]propan-2-ylcarbamate
Homo sapiens
-
pH 7.2, 37°C
13
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
16
(1R,4S)-4-hydroxycyclopent-2-en-1-yl acetate
Homo sapiens
pH and temperature not specified in the publication
-
0.61
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.85
(1S,2R,3S,4R)-4-(2-bromo-6-chloro-9H-purin-9-yl)cyclopentane-1,2,3-triyl triacetate
Homo sapiens
pH and temperature not specified in the publication
-
2.1
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
7.5
(1S,2R,3S,4R)-4-(6-amino-2-methyl-9H-purin-9-yl)cyclopentane-1,2,3-triol
Homo sapiens
pH and temperature not specified in the publication
-
24
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
Homo sapiens
pH and temperature not specified in the publication
-
47.2
1,2-dideoxy-3-O-(ethoxycarbonyl)-6-O-(1H-imidazole-2-carbothioyl)-7-O-[(4-methoxyphenyl)(diphenyl)methyl]-4,5-O-[(1S)-2-(4-methoxyphenyl)ethylidene]-D-allo-hept-1-ynitol
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.07882
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.5
2-((2-((2-(diethylamino)ethyl)amino)-2-oxoethyl)(4-fluorophenyl)amino)-N-(isoindolin-2-yl)-N-methylacetamide
Mycobacterium tuberculosis
-
IC50 above 0.5 mM, at pH 8.0 and 37°C
0.00451
2-aminoaristeromycin
Plasmodium falciparum
-
pH 7.2, 30°C
0.0907
2-aminoaristeromycin
Homo sapiens
-
pH 7.2, 30°C
0.00198
2-fluoroaristeromycin
Plasmodium falciparum
-
pH 7.2, 30°C
0.0472
2-fluoroaristeromycin
Homo sapiens
-
pH 7.2, 30°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
Homo sapiens
-
pH 7.2, 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
pH 7.2, 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.00049
aristeromycin
Mycobacterium tuberculosis
-
at pH 8.0 and 37°C
0.01
aristeromycin
Trichomonas vaginalis
-
pH not specified in the publication, temperature not specified in the publication
4.51
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
20
ethyl (2R,3aR,4S,6R,6aR)-6-([(4-methoxyphenyl)(diphenyl)methoxy]methyl)-2-[(4-methoxyphenyl)methyl]-5-methylidenetetrahydro-2H,3aH-cyclopenta[d][1,3]dioxol-4-yl carbonate
Homo sapiens
pH and temperature not specified in the publication
-
3.3
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
-
18
N-(9-[(1R,4S)-4-hydroxycyclopent-2-en-1-yl]-9H-purin-6-yl)benzamide
Plasmodium falciparum
-
pH and temperature not specified in the publication
-
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
pH 7.2, 37°C
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens
-
at pH 7.2 and 37°C
0.0000015
neplanocin A
Homo sapiens
-
pH and temperature not specified in the publication
0.0000015
neplanocin A
Homo sapiens
pH 6.5, 41°C, recombinant enzyme
0.000047
neplanocin A
Homo sapiens
-
IC50: 47 nM
0.000101
neplanocin A
Plasmodium falciparum
-
IC50: 101 nM
1.1
noraristeromycin
Homo sapiens
pH and temperature not specified in the publication
3.1
noraristeromycin
Plasmodium falciparum
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
drug target
adenosylhomocysteinase inhibitors are promising complementary therapeutic agents in organ transplantation. Inhibitors (AdOx and DZ2002) alleviate allograft rejection in cardiac transplantation by inhibition of CD4+ T alloimmune response
drug target
-
target for antimalarial agents since the parasite has a specific SAH hydrolase. The inhibition of SAH hydrolase causes the intracellular accumulation of S-adenosyl-L-homocysteine (SAH), elevating the ratio of SAH to S-adenosylmethionine (SAM) and inhibiting SAM-dependent methyltransferase that catalyzes methylation of the capped structure at the 5'-terminus of mRNA, and other methylation reaction which is essential for parasite proliferation. In other words, S-adenosyl-L-homocysteine hydrolase regulates methyltransferase reactions. SAH hydrolase inhibitors can be used for the treatment of different diseases like malaria, cancer, viral infection, etc. by ultimately stopping the synthesis of protein
drug target
target for antimalarial agents since the parasite has a specific SAH hydrolase. The inhibition of SAH hydrolase causes the intracellular accumulation of S-adenosyl-L-homocysteine (SAH), elevating the ratio of SAH to S-adenosylmethionine (SAM) and inhibiting SAM-dependent methyltransferase that catalyzes methylation of the capped structure at the 5'-terminus of mRNA, and other methylation reaction which is essential for parasite proliferation. In other words, S-adenosyl-L-homocysteine hydrolase regulates methyltransferase reactions. SAH hydrolase inhibitors can be used for the treatment of different diseases like malaria, cancer, viral infection, etc. by ultimately stopping the synthesis of protein
evolution
S-adenosyl-L-homocysteine hydrolase (SAHH) is one of the most highly conserved enzymes across kingdoms
evolution
-
S-adenosylhomocysteine hydrolase (SAHH) belongs to a large family of proteins that use NAD(P)+/NAD(P)H as cofactors via the dinucleotide-binding Rossmann-fold (a protein structural motif that binds nucleotides, especially the cofactor NAD+)
evolution
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
evolution
evolutionary conserved enzyme governed by multilevel posttranslational control
evolution
evolutionary conserved enzyme governed by multilevel posttranslational control
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH, and the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs. The differences explain the higher NAD+ requirement of tmSAHH because of the reduced affinity and may be related to the thermostability
-
evolution
-
evolutionary conserved enzyme governed by multilevel posttranslational control
-
malfunction
-
down-regulation of enzyme expression impairs sterol synthesis leading to 4fold elevated squalene levels. Yeast mutants lacking the enzyme are viable
malfunction
-
knockout mutants show a phenotype of slower growth rate, fewer aerial hyphae, loss of orange pigment, absence of asexual fruiting bodies and conidia, and a significant reduction in virulence
malfunction
-
complete loss of SAHH is embryonic lethal, whereas SAHH dysfunction results in numerous pathological consequences such as developmental abnormalities, neurovascular disorders, myopathy, cancer and childhood death
malfunction
overexpression of enzyme SAHH in mammalian cells leads to hypermethylation of the genome, whereas its inhibition by adenosine periodate or siRNA-mediated knockdown results in hypomethylation of the genome. Hypermethylation is consistent in both gene bodies and repetitive DNA elements leading to aberrant gene regulation. Cells overexpressing SAHH specifically upregulate metabolic pathway genes and down-regulate PPAR and MAPK signaling pathways genes. Alteration of SAHH level affects global DNA methylation levels and gene expression
malfunction
the inhibition of SAHH can lead to intracellular SAH accumulation, which triggers the negative feedback inhibition to suppress the S-adenosyl-L-methionine (SAM)-dependent transmethylation
malfunction
-
deletion of the enzyme (FgSAH1) results in defects in vegetative growth, asexual and sexual reproduction, stress responses, virulence, lipid metabolism, and tolerance against fungicides
malfunction
-
knockout mutants show a phenotype of slower growth rate, fewer aerial hyphae, loss of orange pigment, absence of asexual fruiting bodies and conidia, and a significant reduction in virulence
-
malfunction
-
deletion of the enzyme (FgSAH1) results in defects in vegetative growth, asexual and sexual reproduction, stress responses, virulence, lipid metabolism, and tolerance against fungicides
-
metabolism
-
treatment with 50 microg/ml N-nitrosomethylbenzylamine results in twenty-eight differentially expressed protein spots in HEEC cells. Two tumor suppressor proteins, prohibitin and c-Myc binding protein, are down-regulated in NMBA-treated HEEC cells. S-adenosylhomocysteine hydrolase, is up-regulated in NMBA-treated HEEC cells
metabolism
the enzyme is involved in the activated methyl cycle (AMC) of mammalian cells, overview
metabolism
DJ-1 depletion inhibits the transsulfuration pathway by disrupting the formation of the S-adenosyl homocysteine hydrolase tetramer and impairing its activity
physiological function
-
transient application of inhibitor 9-(S)-(2,3-dihydroxypropyl)-adenine on tobacco seeds during 6 days during the germination period. The transient drug treatment induces dosage-dependent global DNA hypomethylation mitotically transmitted to adult plants, pleiotropic developmental defects including decreased apical dominance, altered leaf and flower symmetry, flower whorl malformations and reduced fertility, and dramatic upregulation of floral organ identity genes NTDEF, NTGLO and NAG1 in leaves
physiological function
the enzyme catalyzes the breakdown of S-adenosylhomocysteine, a powerful inhibitor of most transmethylation reactions, to adenosine and L-homocysteine
physiological function
-
the enzyme can promote apoptosis, inhibit migration and adhesion of esophageal squamous cell carcinoma cells suggesting that it may be involved in carcinogenesis of the esophagus
physiological function
-
the enzyme is required for virulence and multiple traits of phenotype in Cryphonectria parasitica by regulation of the expression of genes involved in key process of the cell
physiological function
-
the enzyme participates in the regulation of flagellar regeneration of Dunaliella salina
physiological function
the enzyme plays a key role promoting transmethylation reactions in the secondary cell walls biosynthesis in trees
physiological function
DNA methylation generates S-adenosyl-L-homocysteine, a strong inhibitor of DNMT1. S-adenosylhomocysteine hydrolase (SAHH) is the only mammalian enzyme capable of hydrolyzing S-adenosyl-L-homocysteine. SAHH binds to DNMT1 during DNA replication and enhances DNMT1 activity in vitro, DNMT1 and SAHH interact directly during S-phase, overview
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM, S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase
physiological function
S-adenosyl-L-homocysteine hydrolase LvSAHH regulates inflammatory cytokines expression in shrimp
physiological function
-
S-adenosylhomocysteine hydrolase (SAHH) is the only mammalian enzyme capable of hydrolysing S-adenosylhomocysteine (SAH), a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases which methylate diverse cellular components, including DNA, RNA, proteins, lipids and neurotransmitters. SAM-dependent methylation is central to the regulation of numerous biological processes. A wide spectrum of cellular components, including DNA, RNA, lipids, proteins and neurotransmitters, is subjected to methylation by SAM-dependent methyltransferases. SAM serves as the methyl-group donor during transmethylation reactions, yielding S-adenosylhomocysteine (SAH) as a by-product, which is a strong feedback inhibitor of most SAM-dependent transmethylation reactions. In mammals, S-adenosylhomocysteine hydrolase (SAHH) is the only known enzyme that catalyses the hydrolysis of SAH to homocysteine and adenosine, thereby relieving the inhibition. H19 lncRNA alters DNA methylation genome wide by regulating S-adenosylhomocysteine hydrolase. H19 lncRNA knockdown activates SAHH, leading to increased DNMT3B-mediated methylation of an lncRNA-encoding gene Nctc1 within the Igf2-H19-Nctc1 locus. Genome-wide methylation profiling reveals methylation changes at numerous gene loci consistent with SAHH modulation by H19. SAHH interacts with H19 in ribonucleoprotein complexes. Mode of regulation, overview. The SAM-dependent DNA methyltransferase DNMT3B contributes to SAHH-mediated, H19-dependent methylation change in core muscle enhancer (CME), CME methylation correlates with enhanced Nctc1 transcription. SAHH is required for H19-dependent alteration in CME methylation and Nctc1 transcription
physiological function
SAHH plays a critical role in the mammalian methylation processes
physiological function
the enzyme is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions
physiological function
essential enzyme involved in the regulation of cellular S-adenosyl-L-methionine-dependent methylation reactions
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
physiological function
-
S-adenosyl-L-homocysteine hydrolase FgSah1 is required for fungal development and virulence in Fusarium graminearum
physiological function
the enzyme catalyzes the hydrolysis of SAH to homocysteine in the transsulfuration pathway. DJ-1 determines the formation of the S-adenosyl homocysteine hydrolase tetramer and its enzymatic activity by altering the interaction between S-adenosyl homocysteine hydrolase and its negative regulator AHCYL1. DJ-1 depletion inhibits the transsulfuration pathway by disrupting the formation of the S-adenosyl homocysteine hydrolase tetramer and impairing its activity
physiological function
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
physiological function
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
the enzyme is required for virulence and multiple traits of phenotype in Cryphonectria parasitica by regulation of the expression of genes involved in key process of the cell
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase FgSah1 is required for fungal development and virulence in Fusarium graminearum
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
the enzyme is required to maintain trans-methylation reactions in different cellular compartments
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
physiological function
-
S-adenosyl-L-homocysteine hydrolase (SAHase) is a major regulator of cellular methylation reactions that occur in eukaryotic and prokaryotic organisms. SAHase activity is also a significant source of L-homocysteine and adenosine, two compounds involved in numerous vital, as well as pathological processes
-
additional information
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
additional information
overall structure of the inactive form of TmSAHase, overview
additional information
-
overall structure of the inactive form of TmSAHase, overview
additional information
the substrate-binding domain comprises residues 1-181 and 355-385. It is an alpha/beta-type structure consisting of eight alpha-helices and eight beta-strands. The structural core in the domain is an eight-stranded parallel beta-sheet in the centre of the domain that is sandwiched by two arrays of three alpha-helices each. Conformational changes upon substrate binding, overview
additional information
the substrate-binding domain, built from amino acid residues Gly6-Val221 and Met397-Val426, has an alpha/beta-fold. The central parallel beta-sheet is built from seven beta-strands, structure overview. The C-terminal domain, formed by residues Leu427-Tyr473, has a helix-loop-helix-loop fold. Ligand-induced conformational change. Adenosine-binding site in the ligand-free subunit
additional information
-
a coupled photometric assay for characterization of S-adenosyl-L-homocysteine hydrolases in the physiological hydrolytic direction is developed. The assay is a valuable tool for in vitro characterization of SAHases with biotechnological potential, and for monitoring SAHase activity in diagnostics
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
additional information
-
overall structure of the inactive form of TmSAHase, overview
-
additional information
-
both catalytic domain and NAD+-binding domain show a typical alpha/beta twist structure. The core of the catalytic domain is a seven-stranded parallel beta-sheet in the center, which is surrounded by four and three alpha-helices on the two sides. The beta-sheet in the core of the NAD+-binding domain is composed of five parallel and two antiparallel strands, sandwiched by three and two alpha-helices. Structure determination of the unique C-terminal domain of tmSAHH, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystallization is conducted by vapour diffusion in hanging drops at 19°C. Crystal structure is solved at a resolution of 1.74 A, revealing a homotetramer in the asymmetric unit of space group P2(1)2(1)2
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method, using 0.2 M ammonium acetate, 20%(w/v) polyethylene glycol 3350, pH 7.1
purified recombinant detagged enzyme, hanging drop vapour diffusion method, mixing of 12 mg/ml protein in 20 mM Tris, pH 8.0, 50 mM NaCl, with reservoir solution consisting of 0.2 M ammonium acetate, 20% w/v PEG 3350, pH 7.1, 18°C, X-ray diffraction structure determination and analysis at 1.74 A reoslution, molecular replacement using the atomic coordinates of chain A of SAHase from Brucella melitensis (PDB ID 3n58) as template, modelling
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
modeling based on structure from Plasodium falciparum
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
enzyme in ternary complex with the oxidized form of the NAD+ cofactor and adenosine, hanging drop vapor diffusion method, using 15 % (w/v) PEG 8000 and 0.5 M Li2SO4
hanging-drop vapor-diffusion method, crystals are orthorhombic, space group P2(1)2(1)2 with unit cell parameters a = 96.28, b = 102.44, and c = 188.92 A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
hanging drop vapor diffusion method, using 200 mM sodium formate, 5-20% (w/v) PEG 3350, and 100 mM BisTris, pH 6.0-6.5
hanging-drop vapor-diffusion method, complex of the enzyme with neplanocin A
in complex with mechanism-based inhibitor fluoroneplanocin A. The crystallized enzyme complex shows the closed conformation and turns out to be the intermediate of mechanism-based inhibition. The cofactor depletion by 3'-oxidation of fluoroneplanocin A contributes to the enzyme inhibition along with the irreversible covalent modification of enzyme
performance of Brownian dynamics simulations by building a coarse-grained model based on the holo and ligand-bound structures, in order to study the link between the allosteric communication and functional dynamics. Upon ligand-induced transition, the signal of intra-subunit closure dynamics is transmitted to form inter-subunit contacts, which in turn invoke a precise alignment of active site, followed by the dimer-dimer rotation that compacts the whole tetrameric structure. Analysis provides evidence of both induced fit and population shift mechanisms, and also shows that the transition state ensemble is akin to the ligand-bound state. Besides the formation of enzyme-ligand contacts at the active site, the allosteric couplings from the residues distal to the active site is vital to the enzymatic function
purified enzyme in complex with inhibitor N2-[5-chloro-2-(4-chlorophenoxy)phenyl]-N2-[2-[1,3-dihydro-2H-isoindol-2-yl(methyl)amino]-2-oxoethyl]-N1-[2-(methylamino)ethyl]glycinamide hydrochloride, sitting drop vapor diffusion method, using a reservoir solution composed of 100 mM HEPES, pH 7.5, 13% w/v PEG 4000, 10% v/v 2-PrOH, and 0.5% v/v EtOAc, X-ray diffraction structure determination and analysis at 2.7 A resolution, modelling
-
substrate-free wild-type enzyme exhibits reorientational motions on time scales of 10-20 and 80-90 ns. The faster motion is attributed to the domain motion, and the slower motion is attributed to the tumbling of enzyme. The domain motion is present in enzyme complexes with NADH/3'-keto-adenosine and NAD+/3'-deoxyadenosine, but absent in complexwith NADH/3-keto-neplaocin A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystals of LlSAHase in complex with adenosine are obtained by the hanging-drop vapour-diffusion method using 20% (w/v) PEG 4000 and 10% (v/v) 2-propanol as precipitants in 0.1 M Tris-HCl buffer pH 8.0. The crystals are tetragonal, space group P43212, with unit-cell parameters a = 122.4, c = 126.5 A and contained two protein molecules in the asymmetric unit, corresponding to the functional dimeric form of the enzyme. Atomic resolution (1.17 A) X-ray diffraction data are collected using synchrotron radiation
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
using 20% (w/v) PEG 4000, 10% (v/v) 2-propanol, 0.1 M Tris-HCl pH 8.0
-
purified enzyme SAHH in complex with adenosine and with two reaction intermediate analogues, 3'-keto-aristeromycin (3KA) and noraristeromycin (NRN), X-ray diffraction structure determination and analysis at resolutions of 1.55, 1.55, and 1.65 A, respectively
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
to 1.55 A resolution, space group I222
-
crystal structure of SAHH in complex with adenosine (ADO) and nicotinamide adenine dinucleotide and with three inhibitors is shown: 3'-keto aristeromycin, 2-fluoroadenosine, and 3-deazaadenosine. The 3'-keto aristeromycin complex is the first reported structure of SAHH complexed with this inhibitor, and confirms the oxidation of the 3'-hydroxyl to a planar keto group, consistent with its prediction as a mechanism-based inhibitor. The 2.0 A resolution structure of the complex of SAHH cocrystallized with S-adenosylhomocysteine is reported. Binding of homocysteine forces a rotation of His363 around the backbone to flip out of contact with the 5 hydroxyl of the adenosine and opens access to a nearby channel that leads to the surface. This complex suggests that His363 acts as a switch that opens up to permit binding of substrate, then closes down after release of the cleaved homocysteine
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
crystal structure of PfSAHH complexed with the reaction product adenosine. Crystals belong to an orthorhombic space group P2(1)2(1)2(1) with cell dimensions of a = 77.09 A, b = 86.15 A, and c = 333.8 A
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
vapor diffusion method. Crystals belong to an orthothombic space group P2(1)2(1)2(1) with the cell dimensions of a = 76.66 A, b = 86.31 A, c = 335.6 A, four subunits per asymmetric unit, 2.8 A resolution
-
purified recombinant detagged wild-type and mutant enzymes free or in complex with 2'- or 3'-deoxyadenosine, adenosine, or Zn2+, hanging drop vapor diffusion method, 20 mg/ml protein in 100 mM KCl or RbCl, 25 mM HEPES-KOH, pH 7.5, 1 mM TCEP-HCl, mixing with 2 mM of adenosine (Ado/K+/Zn2+), 2'-deoxyadenosine (2'-dAdo/K+/Zn2+ or 2'-dAdo/Rb+), or 3'-deoxyadenosine (3'-dAdo/K+) at 4°C, for crystallization mixing of 0.002 ml of 10 mg/ml protein-ligand solution with 0.002 ml of reservoir solution containing 20% w/v PEG8000 and 50 mM KH2PO4 (Ado/K+/Zn2+ and 2'-dAdo/K+/Zn2+), or 20% w/v PEG8000 and 50 mM RbH2PO4 (2'-dAdo/Rb+), or 15% w/v PEG8000, 50 mM KH2PO4 and 20% v/v glycerol (3'-dAdo/K+), 19°C, X-ray diffraction structure determination and analysis at 1.35 A (3'-dAdo/K+), 1.45 A (2'-dAdo/Rb+), 1.60 A (Ado/K+/Zn2+), or 1.75 A (2'-Ado/K+/Zn2+) resolution, molecular replacement using a subunit of Homo sapiens SAHase as search model (PDB ID 1LI4, chain A)
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
in complex with (2R,3R)-4-(3-deazaadenin-9-yl)-2,3-dihydroxybutanoic acid and NAD+, batch method with 15% (w/v) PEG 8000, 50 mM MES buffer pH 6.5, and 2% (v/v) glycerol
in complex with inhibitor 3-deaza-D-eritadenine
molecular dynamics simulations of substrate-free enzyme in solution. The four substrate-binding domains retain internal structures similar to the crystal conformation. The domains within each subunit fluctuate between open and closed conformations, while at the tetramer level 80% of the domain motions are perpendicular to the direction of the open-to-closed structure transition. Domain reorientation in solution are the sum of a faster and a slower component of 20-50 ps and 8-23 ns, respectively
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
hanging-drop vapor-diffusion method
purified recombinant enzyme free or in complex with adenosine, hanging drop vapour diffusion method, mixing of 0.002 ml of 6 mg/ml protein in 100 mM NaCl, and 25 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 20 mM MgCl2 or CaCl2, 0.1 M sodium acetate, pH 4.6 or pH 5.3, and 30% v/v MPD for crystal structure 1 or 2, respectively, with or without addition of adenosine, 18°C, X-ray diffraction structure determination and analysis at 1.75-1.90 A resolution, molecular replacement using the substrate-binding (residues 18-181 and 355-421) and cofactor-binding (182-354) domains of a model of Homo sapiens SAHase (PDB ID 1LI4) as search model
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 150 mM NaCl, 25 mM Tris-HCl, pH 7.5, 10 mM DTT, and 2 mM NAD+ with 0.001 ml of reservoir solution containing 4.3 M NaNO3, and 0.1 M NaAc, pH 4.6, and equilibration against 0.3 ml of reservoir solution at room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.04 A resolution. Crystals of tmSAHH in complex with both SAH and NAD+ are obtained by soaking and cocrystallization with resolution at 2.85 A. Molecular replacement using the Rattus norvegicus SAHH structure, PDB ID 1B3R, as search model
sitting drop vapor diffusion method, using 0.3 M calcium acetate hydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, and 8% (w/v) polyethylene glycol 8000
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
-
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
-
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
the structural characterization and comparison of S-adenosyl-L-homocysteine hydrolases of eukaryotic and prokaryotic originis is presented. The characterization is based on the crystal structures of SAHases from both, eukaryotic and bacterial enzymes, deposited in the Protein Data Bank
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.