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- exam 4 part 3
exam 4 part 3
Biochemistry 401 with Foley at Michigan State University
About this deck
By: Kara Brockhaus
Textbook: Biochemistry (Looseleaf)
Created: 2010-11-01
Size: 52 flashcards
Views: 32
Textbook: Biochemistry (Looseleaf)
Created: 2010-11-01
Size: 52 flashcards
Views: 32
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Ubiquitin binds to proteins through formation of an __________ bond with _______ residues
isopeptide
Lysine
Lysine
19s subunit does what in a proteosome
target protein is unfolded
what happens in the 20s subunit?
catalytic threonine units attack the peptide bond of the proteint to be destroyed. By making covalent linkages with the peptide backbone, theronine residues hydrolizes the protein into frags of 8-10 AA’s long
Cellular proteins are ______ and _____ by the proteasome
ubiquitinated
degraded
degraded
Proteolysis of Dietary Protein Begins in
the stomach
proteolysis in stomach characteristics
-Pepsinogen: Zymogen (inactive)
- Pepsin: active enzyme
- Non-specific cleavage of protein
- Pepsin: active enzyme
- Non-specific cleavage of protein
- Synthesized and released into stomach
- Activated by low pH
zymogens are
inactive
_____is the only active enzyme (in digestion) made in the _________all others are made in the _________
pepsin
stomach
pancreas
stomach
pancreas
trypsin can _________itself to _________
catalzye
make more trypsin
make more trypsin
pancreatic proteases: characteristics
Enteropeptidase
Oligo-peptides
Oligo-peptides
Released as inactive zymogens
Cleave proteins at specific residues
what does enteropeptidase do?
Activates pancreatic protease cascade
Oligo-peptides that become proteolyzed are called _____ and this occurs _____
aminopeptidases
on luminal surface
on luminal surface
Di- and Tri-peptides cleaved by peptidases in _________
enterocytes.
Amino acids after pancreatic proteases are used in
synthetic reactions, or catabolized
basic strategy of AA catabolism
1.Remove amino group: deamination
2.Remaining carbon skeletons are used:
2.Remaining carbon skeletons are used:
- Energy: Glucose, Acetyl CoA, TCA intermediates
- Anabolic Reactions
fate of AA's
1.converted to urea in urea cycle
2.used for synthesis of nitrogen-containing compounds (i.e. other AA’s or nucleic acids)
2.used for synthesis of nitrogen-containing compounds (i.e. other AA’s or nucleic acids)
catabolic reaction for AA goes like this....
1.Transfer amino group to an a-ketoacid, usually to a-ketoglutarate, to yield glutamate. •
2.•Oxidative Deamination to remove the amino group as ammonium ion.
2.•Oxidative Deamination to remove the amino group as ammonium ion.
what are the two amino transferases?
aspartate amino transferase
alanine amino transferase
*these rxns go in reverse also
alanine amino transferase
*these rxns go in reverse also
what does aspartate amino transferase catalyze?
Aspartate + a-ketoglutarate D OAA + Glutamate
what does alanine amino transferase catalyze?
Alanine + a-ketoglutarate D Pyruvate + Glutamate
7 Carbon skeleton metabolites.
Can be used in these ways
-as anabolic precursors
-to generate energy:
-Glucose (some)
-Acetyl CoA (some)
-TCA Cycle (some)
-to generate energy:
-Glucose (some)
-Acetyl CoA (some)
-TCA Cycle (some)
what are the 7 carbon skeleton metabolites?
Pyruvate
Acetyl CoA
Acetoacetyl CoA
a-Ketoglutarate
Succinyl Co A
Fumarate
Oxaloacetate
Aminotransferases
Require the Prosthetic group:
Pyridoxal Phosphate (VitaminB6 derivative)
characteristics of pyridoxial phosphate
•reactive aldehyde connected to pyrimidine ring
• acts as an electron sink - an electrophilic catalyst
• acts as an electron sink - an electrophilic catalyst
Prior to amino acid binding:__makes protonated Shiff-base with PLP aldehyde thus____
lysine
- Acts as a place-holder for incoming amino acid
- Acts as a place-holder for incoming amino acid
Reactions go in reverse for amination of ketone to
Amino acid
oxidative deamination characteristics
a)Glutamate is oxidized to form a Shiff-base,
b)The amino group is hydrolyzed to yield a free ammonium ion and a-ketoglutarate.
b)The amino group is hydrolyzed to yield a free ammonium ion and a-ketoglutarate.
what catalyzes glutamate to alpha ketoglutarate
glutamate dehydrogenase
Glutamate dehydrogenase is found where?
mitochondria
ammonium is
toxic
glutamate ---> alpha keto glutarate can use ____ or _____
NAD--> NADH
OR
NADP--> NADPH
OR
NADP--> NADPH
what inhibits
Glutamate dehydrogenase
ATP or GTP
what activates
Glutamate dehydrogenase
ADP
or
GDP
or
GDP
___ and ____can be Directly Deaminated
serine and theroine
Serine---serine dehydrogenase--->
Pyruvate + NH4+
theroine ---deamination--->
a-Ketobutyrate + NH4+
muscles can use what branced chain AA's for fuel?
Ile
Leu
Val
Leu
Val
muscles do not have _____ enzymes to process ammonium
urea cycle
muscles needs to send amino grps to liver via
alanine
(sometimes glutamine)
(sometimes glutamine)
Ammonium excreted (through the kidneys in most cases) as urea by most land animals.
- Exceptions=
birds, reptiles, amphibians
in the urea cycle what is given off?
–1 N from NH4+
–1 N from aspartate
–C from bicarbonate
–1 N from aspartate
–C from bicarbonate
aquatic animals excrete ____into the water
NH4+
birds and reptiles excrete
uric acid
basic strategy of urea cycle
Get rid of the NH4+ safely as urea
Salvage the Carbon skeleton metabolites for use as fuel or building blocks
urea cycle begins in __________and last 3 rxns occur in _______
mitochondria
cytosol
cytosol
steps of the urea cycle in the mitochondrial matrix
a) Activation of Bicarbonate with ATP, to form Carboxyphosphate
b) Condensation of Carboxyphosphate with Ammonia
c) Activation of carbamic acid with ATP to form Carbamoyl Phosphate
what catalyzes citrulline + aspartate --> argininosuccinate
*argininosuccinate synthetase
*ATP is needed along with the release of PP
*ATP is needed along with the release of PP
argininosuccsuccinate ---> arginine + fumarate is catalyzed by....
argininosuccinase
argine--> ornithine +urea is catalyzed by
arginase
___________ is Transported from Cytosol To MT to Join the Urea Cycle
ornithine
4 fates of OAA
1.Transamination to make Aspartate
2.Condensation with Acetyl CoA to make Citrate > energy (TCA cycle) 3.Gluconeogenesis > energy export
4.Conversion to pyruvate then to acetyl Co A for FA synthesis
2.Condensation with Acetyl CoA to make Citrate > energy (TCA cycle) 3.Gluconeogenesis > energy export
4.Conversion to pyruvate then to acetyl Co A for FA synthesis
The urea and TCA cycle have what direct intermediate in common
fumarate
About this deck
By: Kara Brockhaus
Textbook: Biochemistry (Looseleaf)
Created: 2010-11-01
Size: 52 flashcards
Views: 32
Textbook: Biochemistry (Looseleaf)
Created: 2010-11-01
Size: 52 flashcards
Views: 32
About StudyBlue
STUDYBLUE makes things that make you better at school.
Things like online flashcards with photos and audio.
Things like personalized quizzes and friendly reminders about when (and what) to study next.
Think of it as a digital backpack™: access to all of your study materials online and on your phone.
STUDYBLUE exists to make studying efficient and effective for every student, for free. Join us.
“I have been getting MUCH better grades on all my tests for school. Flash cards, notes, and quizzes are great on here. Thanks!”
Kathy
Kathy