Glycolysis
Glycolysis
Glycolysis
Step 1: Hexokinase
The reaction occurs with the help of the enzyme hexokinase, an enzyme that
catalyzes the phosphorylation of many six-membered glucose-like ring
structures. Atomic magnesium (Mg) is also involved to help shield the negative
charges from the phosphate groups on the ATP molecule. The result of this
phosphorylation is a molecule called glucose-6-phosphate (G6P), thusly called
because the 6′ carbon of the glucose acquires the phosphate group.
Step 3: Phosphofructokinase
The enzyme Aldolase splits fructose 1, 6-bisphosphate into two sugars that are
isomers of each other. These two sugars are dihydroxyacetone phosphate (DHAP)
and glyceraldehyde 3-phosphate (GAP).
Details: This step utilizes the enzyme aldolase, which catalyzes the cleavage of
FBP to yield two 3-carbon molecules. One of these molecules is called
glyceraldehyde-3-phosphate (GAP) and the other is called dihydroxyacetone
phosphate (DHAP).
Details: GAP is the only molecule that continues in the glycolytic pathway. As a
result, all of the DHAP molecules produced are further acted on by the enzyme
Triosephosphate isomerase (TIM), which reorganizes the DHAP into GAP so it
can continue in glycolysis. At this point in the glycolytic pathway, we have two 3-
carbon molecules, but have not yet fully converted glucose into pyruvate.
The enzyme GAPDH contains appropriate structures and holds the molecule in a
conformation such that it allows the NAD molecule to pull a hydrogen off the
GAP, converting the NAD to NADH. The phosphate group then attacks the GAP
molecule and releases it from the enzyme to yield 1,3 bisphoglycerate, NADH, and
a hydrogen atom.
Details: This step involves a simple rearrangement of the position of the phosphate
group on the 3 phosphoglycerate molecule, making it 2 phosphoglycerate. The
molecule responsible for catalyzing this reaction is called phosphoglycerate mutase
(PGM). A mutase is an enzyme that catalyzes the transfer of a functional group
from one position on a molecule to another.
The reaction mechanism proceeds by first adding an additional phosphate group to
the 2′ position of the 3 phosphoglycerate. The enzyme then removes the phosphate
from the 3′ position leaving just the 2′ phosphate, and thus yielding 2
phsophoglycerate. In this way, the enzyme is also restored to its original,
phosphorylated state.
Step 9: Enolase
Details: