EC Number   |
Inhibitors |
Structure |
|---|
    1.5.1.20 | (+)-5-methyl-5,6,7,8-tetrahydropteroylpentaglutamate |
inhibits at high concentrations |
   |
| 1.5.1.20 | (S)-SKI-72 |
binds MTHFR via its allosteric domain with nanomolar affinity. Assay of MTHFR activity in the presence of (S)-SKI-72 demonstrates inhibition of purified enzyme with submicromolar potency and endogenous MTHFR from HEK293 cell lysate in the low micromolar range, both of which are lower than AdoMet. Nevertheless, unlike AdoMet, (S)-SKI-72 is unable to completely abolish MTHFR activity, even at very high concentrations |
|
| 1.5.1.20 | (S)-SKI-73 |
a (S)-SKI-72 prodrug derivative, in which the 9'-amine moiety is cloaked with the trimethyl-locked quinone butanoate moiety, on intact HEK293 cells. Once (S)-SKI-73 passes inside the cell membrane, it is metabolised into (S)-SKI-72 and 60-N benzylhomosinefungin, which then accumulates inside the cell |
|
| 1.5.1.20 | 2,4-dihydroxyphenylacetic acid |
at 0.01 M |
|
| 1.5.1.20 | 5,10-methylenetetrahydrofolate |
substrate inhibition |
|
| 1.5.1.20 | 5,10-methylenetetrahydrofolate |
- |
|
| 1.5.1.20 | dicoumarol |
inhibits menadione reductase activity only |
|
| 1.5.1.20 | diethyldicarbonate |
20 mM NADP+ and 20 mM NAD+ partially protected the enzyme against inactivation whereas 20 mM nicotinamide gives complete protection |
|
| 1.5.1.20 | dihydrofolate |
competitive with respect to 5,10-methylenetetrahydrofolate and uncompetitive with respect to NADPH |
|
| 1.5.1.20 | dihydrofolate |
- |
|
