Debate and discussion of any biological questions not pertaining to a particular topic.
I understand that an enzyme-substrate must be formed for an end prduct to be produced, but how might an inhibitor reduce the effectiveness of an enzyme? Would it be because an inhibitor slows down the normal turnover number of an enzyme because it does not allow the normal substrate to have access to the enzyme?? Help....
Have a look at these:
Hope they help...
It matters not how strait the gate
How charged with punishment the scroll
I am the Master of my fate
I am the Captain of my soul.
I love my analogies so I'm going to use another one here
If an enzyme is a lock...
And a molecule an enzyme is supposed to react with is a key...
Then an inhibitor is when you put Krazy Glue into the lock. That way, when the person who's car you just vandlized tries to put his key in the lock, he can't.
Nice analogy, biostudent. I love analogising to:)
"As a biologist, I firmly believe that when you're dead, you're dead. Except for what you live behind in history. That's the only afterlife" - J. Craig Venter
Science is the art of comparing things. Even quantitative analysis....you compare things to how long a centimeter is =). I find that analogies help. Sometimes I'm lucky and an analogy will explain an idea perfectly...even it if doesn't it will at least give you a general idea =)
Not perfectly exact, though. There are different kind of inhibition.
Inhibitor is a key that fit iside the lock, but does not open it, and even sometimes cannot get out anymore. It slows down the enzyme because molecules have to compete with one another for the active site. The more inhibitor the less enzyme activity.
Inhibitor is the garage door. It is not competing with the substrate for the fixation site, it just blocks the acces to the active site for the substrate.
Analogies aren't meant to be exact. They're meant to give a basic understanding of what's going on. The simpler an analogy is, the easier it is to understand. I wouldn't exactly expect Diana Timpano to write an entire paper on the analogy...but it would give her enough understanding to find other sources of information.
Right, but I simply wanted to say that your analogy was a little too simple.and sort of misleading.
I did not want to hurt you though, just be a little more precise. So Sorry if you thought that I was too hard on you.
Is this the same as non-competitive inhibition? It's not competing for the active site but the name's thrown me slightly!
Non-competitve inhibitors change the overall shape of the enzyme so the 'key' can't even fit in the 'lock.' I am thinking along the right lines aren't I?
I intend to live forever, so far so good!
No, I'm not insulted. However I do find it highly amusing that the only time you post in this forum is to knit-pick qualitative analysis.
I just found that your analogy was too general and was really missing half the problem (allosteric enzymes) Other wise it would have been fine with me> And I really love to find truely good analogies...
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