Exam 3 Review Flashcards
Glycolysis Step 2
G6P –> F6P
phosphoglucose isomerase
Glycolysis Step 1
glucose –> G6P
Hexokinase
Irreversible, USE 1 ATP
Glycolysis Step 3
F6P –> F-1,6-BP
PFK 1
Irreversible, USE 1 ATP
Glycolysis Step 4
F-1,6-BP –> glyceraldehyde 3-P
Aldolase
Glycolysis Step 5
glyceraldehyde 3-P –> DHP
triose phosphate isomerase
Glycolysis Step 6
glyceraldehyde 3-P –> 1,3-BPG
“ “ dehydrogenase
NAD+ –> NADH
Glycolysis Step 7
1,3-BPG –> 3-PG
phosphoglycerate kinase, GAIN 1 ATP
Glycolysis Step 8
3-PG –> 2-PG
Phosphoglycerate mutase
Glycolysis Step 9
2PG –> phosphoenolpyruvate
enolase, lose H20
Glycolysis Step 10
phosphoenolpyruvate –> pyruvate
PKA, GAIN 1 ATP
irrerversible
What regulates pdh in high energy charge (-)?
high NADH, high ATP, high acetyl CoA
pyruvate will NOT continue to CAC
what regulates PDH low energy charge (+)
high pyruvate, high ADP will allow pyruvate to enter CAC
isocitrate dehydrogenase regulation (+) and (-)
+ high ADP, allosterically stimulates
- high ATP, NADH inhibits
alpha-ketoglutarate dehydrogenase regulation -
- high ATP, and allosterically inhibited by its products, NADH and succinyl CoA
- similar to PDH
what does a competitive inhibitor do and how does it affect Vmax and Km?
binds to active site and blocks substrate
Vmax unchanged
Km increases
What does an uncompetitive inhibitor do and how does it affect Vmax and Km?
binds to adjacent site after substrate binding (ES –> ESI)
Vmax and Km changed but slope of lineweaver-burke is unchanged
Km lowers as the concentration of inhibitor increases
What does a non-competitive inhibitor do and how does it affect Vmax and Km?
binds allosterically to E and/or ES complex
Vmax is decreased and cannot be obtained
Km is unchanged
zymogen
inactive protease
enteropeptidase
cleaves to activate zymogen
what enzyme is synthesized in stomach?
pepsin
what enzymes are synthesized in the pancreas?
chymotrypsin, trypsin, procarboxypeptidase, proelastase
