Would anyone know if the inhibition of the maleate ion on Glu-OAA transaminase is covalent or not?

if it's covalent does it attack the aldehyde form or the amine form of PLP?

Question

Would anyone know if the inhibition of the maleate ion on Glu-OAA transaminase is covalent or not?

if it's covalent does it attack the aldehyde form or the amine form of PLP?

abb0t · Answer

Yes it's covalent, and yes it would attack the aldehyde. protinate the carbonyl O and deprotinate the amine...form the schiff base between the amine and carbonyl...

When I get home I can show you the mechanism on paper if you're still interested. I'm pretty sure I stil have my notes lying around somewhere.

aaronq · Answer

oh sweet, thanks. I have the mechanism, i'm just not sure how maleate binds to the active site. so are you talking about the amine from the lysine R group? Kinda like this?

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abb0t · Answer

Yeah, but it binds to the amine group on the lysine group after it attaches itself to the PLP.

abb0t · Answer

it attacks the aldehyde group on the pyroxal forming e-lysyl pyridoxoamine, if i remember correctly.

aaronq · Answer

awesome. i looked everywhere on the net and couldn't find that detail. thanks a lot man