Chapter 17
Glycolysis
Glucose (sugar) is an excellent fuel - input of glycolysis
good amount of energy upon oxidation
efficiently stored in polymeric form
many organisms/tissues can meet energy needs on glucose only
Glucose is a versatile biochemical precursor (carbon source)
bacteria use glucose to build carbon skeletons
amino acids, membrane lipids, nucleotides, cofactors for metabolism
synthesis of structural polymers, storage, oxidation via pentose phosphate pathway, and oxidation via glycolysis
Glycolysis: sequence of enzyme-catalyzed reactions
glucose is converted into pyruvate
pyruvate can be further aerobically oxidized if oxygen present
pyruvate can be used as precursor in biosynthesis
oxidation free energy is captured by synthesis of ATP and NADH
Research of glycolysis plays large role in development of modern biochemistry
role of coenzymes and ATP (energy), methods for enzyme purification
No requirement for oxygen
anaerobic metabolism was most important for first years of life on earth
aerobic organisms generate precursors for aerobic metabolism
useful for short-term energy production when oxygen is limiting
during intense activity, the heart cannot supply sufficient oxygen
glucose is converted anaerobically to lactate
lactate: acid - buildup causes muscles to be sore
Preparatory phase: conversion of glucose to glyceraldehyde-3-phosphate
phosphorylation of glucose to give glucose-6-phosphate
irreversible due to large ∆G’º with a negative value
driven in direction of G6P by 2ATP
hexokinase binds ATP and glucose to prime glucose-6-phospate
first regulatory step of glycolysis
isomerization of glucose-6-phosphate to give fructose-6-phosphate
reversible due to positive ∆G’º
glucose becomes fructose via phosphohexase isomerase
phosphorylation of fructose-6-phosphate to give fructose-1,6-biphosphate
cleavage of fructose-1,6-biphosphate to give glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP)
isomerization of dihydroxyacetone phosphate to give glyceraldehyde-3-phosphate
Reaction 1: ATP-dependent phosphorylation of glucose
nucleophilic oxygen at C-6 of glucose attacks y-phosphorus of ATP
traps glucose in the cell
lowers intracellular glucose concentration
facilitates glucose into the cell
Hexokinase: shows structural change upon binding of glucose
two domains of the protein move closer together
bring ATP closer to C-6 of glucose
exclude water from active site
prevent hydrolysis of ATP
four hexokinase isozymes are found in humans
I-III have similar properties
high affinity for glucose
hill number = 1.0 (positive cooperativity)
allosterically inhibited by product (glucose-6-phosphate)
IV (glucokinase) found in liver with different properties
low affinity for glucose
hill number = 1.5 (positive cooperativity)
no product inhibition
liver does not need to feed glucose in glycolysis when blood glucose is normal
when blood glucose is high, liver can function to feed extra glucose into glycolysis
Reaction 2: Formation of fructose-6-phosphate from glucose-6-phosphate
reversible - positive ∆G’º
Reaction 3: ATP-dependent phosphorylation of fructose-6-phosphate
ATP is donor of second phosphate group
second priming reaction with phosphofructokinase-1 (PFK-1) enzyme
irreversible - committed step in glycolysis
product (fructose-1,6-biphosphate) is committed to become pyruvate
complex regulatory pattern - PFK-1
PFK-1 is inhibited by ATP and citrate (citric acid cycle)
PFK-1 is activated by AMP, ADP, and fructose-2,6-biphosphate
PFK-1 is inhibited when ATP is high and activated when ATP is low
Reaction 4: Cleavage of fructose-1,6-biphosphate into two triose phosphates
fructose-1,6-bisphosphate: aldolase enzyme
cleaves aldol into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate
Reaction 5: Interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P)
only glyceraldehyde-3-phosphate is a substrate for the remaining reactions of glycolysis
important to interconvert DHAP and G3P
triose phosphate isomerase enzyme converts DHAP to G3P
Summary for first phase of glycolysis
glucose converted to 2 molecules of glyceraldehyde-3-phosphate
key intermediate is ATP-dependent phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate (reaction 3)
phosphofructokinase-1 enzyme catalyzes reaction
subject to allosteric control
Payoff phase of glycolysis: 2 simultaneous processes
Reaction 6: Formation of 1,3-biphosphoglycerate
first energy-yielding step in glycolysis
glyceraldehyde-3-phosphate dehydrogenase enzyme
oxidation of aldehyde with NAD+ gives NADH
Arsenic poisoning: arsenate is a phosphate analog and can serve as an alternate substrate (can attack same spot as phosphate)
uncouples glucose oxidation from phosphorylation
Reaction 7: Substrate level phosphorylation of ADP and formation of 3-phosphoglycerate
1,3-biphosphoglycerate is a high energy compound that can donate the phosphate group to ADP to make ATP
phosphoglycerate kinase enzyme
glucose is cleaved into 2 3-carbon fragments
net ATP yield from glycolysis is zero to this point
subsequent reactions generate a net GAIN in ATP
Reaction 8: Isomerization of 3-phosphoglycerate (transfer phosphate to C-2)
isomerization to form 2-phosphoglycerate
active site phosphorylated His required for catalysis
phosphoglycerate mutase enzyme
Reaction 9: Dehydration of 2-phosphoglycerate (create double bond)
a,ß-elimination of H2O
enolase enzyme
chemical logic: create a better phosphoryl donor
Reaction 10: Substrate level phosphorylation #2 and conversion of PEP to pyruvate (phosphoenolpyruvate to pyruvate)
net ATP yield is 2ATP/glucose
pyruvate kinase enzym
subsequent aerobic oxidation of glucose by other metabolic pathways generates additional ATPs/glucose
Glycolysis summary
10 reactions
three of the 10 exhibit large negative ∆G’ and are the sites of regulation
hexokinase (reaction 1)
PFK-1 (reaction 3)
pyruvate kinase (reaction 10)
Pyruvate kinase is subject to regulation
allosterically activated by AMP and fructose-2,6-biphosphate
allosterically inhibited by ATP and acetyl-CoA
requires divalent metals for activity
limited by level of Mg++
when there is plenty of ATP, Mg ions are sequestered by ATP
slows pyruvate kinase
Glycolysis and Cancer
Metabolism in tumor cells is largely anaerobic
glycolysis occurs at elevated rates in tumor cells
yields far less ATP than complete oxidation to carbon dioxide that takes place in healthy cells under aerobic conditions
tumor cell must consume more glucose to produce same amount of ATP
glucose transporters and glycolytic enzymes are overproduced
compounds that inhibit hexokinase, glucose 6-phosphate dehydrogenase, or transketolase block ATP production by glycolysis
depriving cancer cell of energy and killing it
Phosphorylation of 18F-labeled 2-fluoro-2-deoxyglucose by hexokinase traps FdG in cells where is can be detected by positron emission from 18F
CT shows cancer in various areas of the body including the bladder which excretes 18F-labeled compounds
Entry of galactose into glycolysis
inability to convert galactose to glucose leads to human disease
galactosemia - characterized by high blood galactose concentration
symptoms: failure to thrive, mental retardation, cataracts, and death from liver disease
treatment: eat galactose-free diet
defects in all three enzymes are known
most common and most severe is mutation in UDP-glucose:galactose 1-phosphate uridyltransferase
Metabolic fates of pyruvate
regeneration of NAD+
if NADH is not recycled back to NAD+, glycolysis cannot run
NAD+ is required in the oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate (reaction 6)
if oxygen is available, NADH is re-oxidized by the electron transport chain leading to complete oxidation to carbon dioxide and reduction of oxygen to water
if oxygen is unavailable, NADH is re-oxidized by reduction of pyruvate to either lactate or ethanol
pyruvate to lactate - animal tissues
catalyzed by lactate dehydrogenase
carbonyl of pyruvate is transformed to lactate
lactate builds up in muscles during strenuous exercise
acidification prevents continuous strenuous work
lactate can be transported to liver and converted to glucose there
pyruvate to ethanol - yeast
requires Mg++, thiamine pyrophosphate with pyruvate decarboxylase
requires Zn++ and NAD+ with alcohol dehydrogenase
ester group of pyruvate is transformed to ethanol
Summary
pyruvate is converted to lactate in anaerobic tissues
actively metabolizing muscle
NAD+ is recycled
pyruvate is converted to ethanol in yeast
requires thiamine pyrophosphate as coenzyme
NAD+ is recycled