Main content
MCAT
Course: MCAT > Unit 5
Lesson 2: Enzyme structure and function- Enzyme structure and function questions
- Enzyme structure and function
- Introduction to enzymes and catalysis
- Enzymes and activation energy
- Induced fit model of enzyme catalysis
- Six types of enzymes
- Co-factors, co-enzymes, and vitamins
- Enzymes and their local environment
© 2023 Khan AcademyTerms of usePrivacy PolicyCookie Notice
Co-factors, co-enzymes, and vitamins
Co-factors and co-enzymes assist enzymes in their function. We will learn what both co-enzymes and co-factors are, and how they might affect the catalysis of a reaction. By Ross Firestone. Created by Ross Firestone.
Want to join the conversation?
- what is apoenzyme and holoenzyme?(14 votes)
- Simply put, apoenzymes are the protein portion of an enzyme, once they’re bound to a cofactor they become active, becoming holoenzymes.(16 votes)
- This video never clarifies that cofactors and coenzymes are non-protein by definition. This actually shows up in one of the questions for this section.
Also, this video give the impression that coenzymes and cofactors are different things, but coenzymes are a type of cofactor.(14 votes)- I agree with joseph, they should redo this video. Coenzymes should be classified as a type of cofactor, the same way BMW is classified as a type of a car. There are two types of coenzymes, cosubstrates (like NAD+) and prosthetic groups (like heme). Ref. Principles of Biochem textbook (moran et al.)(15 votes)
- What is the actual definition of "organic"?(4 votes)
- An organic molecule is one that contains carbon atoms / is carbon based.(21 votes)
- Are co-factors and co-enzymes considered enzymes?(6 votes)
- No. I would think of them as enzyme helpers. Enzymes are usually big proteins made by your cells while cofactors and coenzymes are small and often can't be made by your cells.(11 votes)
- how to increase testosterones level in your body(1 vote)
- What type of biological molecule category would co-factors and co-enzymes fall under? are they a mix?(4 votes)
- Both are non-protein molecules that can be organic or inorganic helpers of proteins (they are not necessarily always helping enzymes but often do). All coenzymes technically are also cofactors but not all cofactors are coenzymes. Co-enzymes are usually loosely bound and organic. Subcategories such as prosthetic groups (ex. Heme) refer to how tightly bound the cofactor is. Prosthetic groups are tightly bound usually via covalent bonds. The term cosubstrate means loose/diffusible and needed in stoichiometric amounts.(6 votes)
- Is NADH a substracte or Co-enzyme just based on the perspective taken?(2 votes)
- It's a co-enzyme. Lactate Dehydrogenase uses NAD+/NADH as a co-enzyme (its organic!) to convert between pyruvate and lactate.(4 votes)
- atMg2+ is shown to be stabilising a molecule of DNA. It was shown to be stabilising 3 negative charges on the molecule, however there is only two positive charges on the magnesium, how is it able to balance three negative phosphate ions? 3:35(3 votes)
- Isn't iron in hemoglobin a co-factor, that simply acts as a carrier of oxygen? Is it accurate to say that a distinction between the two is that co-factors don't act as just carriers?(2 votes)
- Some sources, like here, limit the use of the term "cofactor" to inorganic substances only. Others divide cofactors into several subgroups that becomes more all encompassing.
Cofactors can be subdivided into either one or more inorganic ions, a complex organic or metalloorganic molecule called a coenzyme.
The iron in heme acts as a prosthetic group. Heme is therefore sometimes referred to as a Metalloprotein. Metalloprotein is a generic term for a protein that contains a metal ion cofactor. You'll see characteristics of both coenzymes (organic) and cofactor (inorganic) attributes. Not necessarily one or the other.
Hope this helps.(3 votes)
- Are cofactors/coenzymes considered allosteric regulators?(1 vote)
- Typically if a molecule is acting on an enzyme allosterically, it is not considered an co-factor, it would be considered a cell signaling molecule. Often times calcium is bound to an enzyme through a molecule known as calmodulin. This interaction alters the functions of proteins. Some examples of these interactions are found in the adenylate kinase or nitric oxide synthase pathways.(1 vote)
Video transcript
Today, we're going to talk
about co-factors and co-enzymes and how sometimes
they can be essential to proper enzymatic function. But first, let's review
the idea that enzymes make reactions go faster. And they do this by lowering
the activation energy peak of their
respective reactions. Let's also review the idea that
enzymes bind their substrates at a location on the enzyme
called the active site, which is where most of the
reaction takes place. Now, not all enzymes are
able to catalyze reactions on their own. And some need a little help. So if we have our
enzyme here, trying to react with our
substrate over here, sometimes something
called a co-factor or a co-enzyme will be
needed, which will also need to bind to
the enzyme in order for it to function properly. And we're going to go over what
co-enzymes and co-factors are and exactly how they work. So first, we'll talk
about what a co-enzyme is. Well, co-enzymes are
organic carrier molecules. And what I mean by "organic"
is that they're primarily carbon-based molecules. And by "carrier," I
mean that co-enzymes hold on to certain
things for an enzyme to make the catalysis run
a little more smoothly. And a great example
of a co-enzyme is NADH, which acts as
an electron carrier. And here, I've shown NADH
dissociating into its oxidized form, NAD+, as well
as to a hydride ion, which basically just exists as
a pair of electrons that some other molecule
would be grabbing. So NAD+ can accept electrons,
causing the molecule to be converted to NADH, which
could then carry electrons for an enzyme. Now if you remember the lactic
acid fermentation reaction, where pyruvate is
converted to lactic acid, you'd see that the
enzyme catalyzing this reaction,
lactate dehydrogenase, uses NADH as a co-enzyme in
order to transfer electrons to the pyruvate
molecule, in order to turn it into lactic acid. And in this sense,
NADH is acting as an electron-carrying
co-enzyme. Another example of a
co-enzyme is co-enzyme A, which like NADH acts
as a carrier molecule. But instead of carrying
electrons like NADH does, co-enzyme A, which we
sometimes call CoA, holds on to acyl or
acetyl groups instead. And you'd see CoA appear quite
often in metabolic reactions, where it will carry
these two carbon acetyl groups from one
molecule to another. Now, co-factors are a little
different from co-enzymes. While co-enzymes are
only really involved in transferring different things
from one molecule to another, co-factors are directly
involved in the enzyme's catalytic mechanism. They don't strictly
carry something like a co-enzyme
would, but might be stabilizing the
enzyme or the substrates or helping the reaction
convert substrates from one form to another. A great example of this is
with the enzyme DNA polymerase. Remember that DNA polymerase
is responsible for helping out with synthesizing new DNA
during DNA replication. Now, you may
remember that DNA is a very negatively charged
molecule because of all the negatively charged phosphate
groups that you'll find around it. Well, DNA polymerase
uses a magnesium ion as a co-factor, which can
use its big positive charge to stabilize all that
negative charge on DNA. And you can see how this is
different from a co-enzyme. Becomes instead of acting as a
carrier molecule, the magnesium ion co-factor is
stabilizing the DNA and is more directly involved
in the actual catalysis. Now, interestingly,
what people normally called vitamin and
minerals, like the kinds that a doctor would
tell you to make sure you get enough
of in your diet, are often different
co-factors and co-enzymes. And what's special about
vitamins and minerals is that your body can't
build them up from scratch. And you need to get
them from your diet in order to stay healthy. So when we say
vitamins, we typically refer to organic
co-factors and co-enzymes. So two great examples are
ones we just discussed. Vitamin B3, which you may
see being called niacin on a food label, is actually
just a precursor for NAD. And vitamin B5 is just a
precursor for co-enzyme A. Minerals, on the other
hand, are inorganic, meaning they aren't
carbon based. And minerals are usually
just co-factors in our body. So magnesium would be a great
example of a mineral co-factor that an enzyme like DNA
polymerase would use. Now, not all minerals
act only as co-factors. Some minerals, like calcium,
which can act as a co-factor, is also a critically important
component of bone and teeth. And it doesn't strictly act
as an enzyme co-factor here. It's actually an important
part of the structure itself. So what did we learn? Well, first we learned
that not all enzymes are able to function alone and
some need a little help. And next, we learned
that this help can come from co-enzymes,
which usually act as carrier molecules, or co-factors,
which directly assist with the catalysis that
the enzyme is doing. And finally, we learned that the
vitamins and minerals generally refer to dietary
co-factors and co-enzymes.