In the function of an aminotransferase enzyme after the first substrate (amino acid) has been deaminated there seem to be nothing binding the resulting pyridoxamine phosfate to the rest of the enzyme (thus defying the definition of prosthetic group). So what keeps it inside the active site of the enzyme so that it is ready to donate the amino group when the second subtrate binds? Bonus question: what keeps the lysine bound to the pyridoxal phosphate (internal aldimine) from losing a proton and becoming a quinonoid intermediate itself?
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$\begingroup$ What research have you done on your own to answer this question? The Biology.SE community has agreed that questions that show little or no prior research effort are off-topic on this site unless you have shown your attempt at an answer. Please edit your question and tell us where you've looked for answers, what you do know about the topic, and where exactly you still have questions. Our goal is not simply to be an answer site, but rather a site that promotes self-learning with some expert help along the way. $\endgroup$– MattDMoJan 17 at 14:22
1$\begingroup$ Reading everything my course's book (Lehninger's Priciples of Biochemistry) has to say about aminotransferase enzymes in my opinion counts as an attempt to get an answer. And it seemed to me that the question was specific enough to show that I've done a bit more than little or no prior research. If this is not enough thanks for the info, I didn't know that. $\endgroup$– AlexanderCarJan 19 at 17:53
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