Final extras Flashcards
What is a exo- and endoprotease?
Exoproteases cleave a protein at its ends; aminopeptidase and carboxypeptidase
Endoprotease cleace within a protein
Which two amino acids has two chiral chains?
Threonine and isoleucine
Which AA has a charges sidechain at pI?
Argenine and lysine
What are characteristic for alpha chains?
Maximum amount of H-bonds. 3.6 residues per turn. Most often right handed. Primary structure in alpha-keratin. H-bond between residue 1 and 4. Sidechain are pointet out.
Glycine and proline decreases its stability (there are many other factors..)
What are characteristic for beta sheets?
H-bonds are either in line parallel or anti-parallel.
What are characteristic for beta-turns?
Reverse the direction of the polypeptide chain. 4 amino acids. 1st AA carbonyl oxygen forms H-bond with 4 AA amino group.
Proline and glycine often occur in B-turns.
Which interactions are important for a proteins tertiary structure?
Disulfide bonds Hydrophobic AA at the interior H-bonds between polar AA Ionic interactions Hydrophilic surface
What is the normal AA code in collagen?
Gly-X-Y, where X and Y is proline and hydroxyproline (or hydroxylysine)
Keratin consists of how many strands?
Two. Create a left-handed helix. Rich in hydrophobic AA (not proline)
List 5 general facts about enzymes
Activation energy decreases Delta G does not change The reaction mechanism change Eq state does not change Time to reach EQ is decreased
A nucleotid are made up by? What are the name of the bond between two nucleotids?
a nitrogenous base, a five-carbon sugar (ribose or deoxyribose), and one phosphate group.
3´5´ phosphodiesterbond (3carbon on one ribose to a 5 carbon on the other ribose)
What bases do we have?
Purine: Guanine, adenine
Pyramidines: Thymine, cytosine
Adenine and thyme + Cytosine and Guanine has how many H-bond
A-T = 2 C-G = 3
RNA when formed is first “protected” by modification of the 3 and 5 end by what?
3 end = poly adenine groups. 200+
5 end = Cap (methylated guanine triphosphate)
What is typical about Scurvy?
Scurvy is a disease resulting from a deficiency of vitamin C. Humans and certain other animal species require vitamin C in their diets for the synthesis of collagen
Replication of DNA occur in which stage of the cell cycle?
S-phase
Describe these stages, G1, S, G2, M in the cell cycle
G1 = prepare to duplicate S = synthesis of DNS G2 = prepare for cell division M = cell division
G0 = “cell rest”
DNA polymerase read and make nucleotides in what direction?
Read: 3-5
Make DNA: 5´-3´
What is the name of the antibiotic that work on prokaryotic RNA synthesis?
Rifampicin
Anomers
Isomeric form of monosaccarides that differ in the conformation around the hemiacetal or hemiketal carbon bond, known as a anomeric carbon
alpha and beta conformation
Epimer
Two sugars that differ only around one carbon.
E.g. Glucose and mannose is C4 epimers
What is the bond name between two monosaccarides? What monosaccarides is present in maltose, lactose and sucrose?
Glycosidic bond. 1-4 linkage
Maltose = 2x glucose - alpha 1-4 Lactose = Glucose + galactose - beta 1-4 Sucrose = Glucose + fructose - beta 2 - alpha 1
What is the difference between amylose and amylopectin? That is special about cellulose?
Amylose has only alpha 1-4 bonds
Amylopectin is “plant glycogen”. Has 1-6 branching points
Cellulose can not be broken down in the GI- tract. We dont have enzymes that can act on beta 1-4 bonds.
What is the function of telomerase?
Elongate the ends of DNA strands (telomer). E.g. after DNA replication
Histones and its modifications
Octamers (4 dimers). H1 linkage. Positive charged (arginine + lysine). Makes DNA more condense. Nucleosome -> Nucleofilaments.
HAT (histone acetyl transferase) decondese
HDAC (histone deacetylase) condense
Topoisomerase function and types
Topoisomerases are enzymes that regulate the overwinding or underwinding of DNA. The winding problem of DNA arises due to the intertwined nature of its double-helical structure. During DNA replication and transcription, DNA becomes overwound ahead of a replication fork. If left unabated, this torsion would eventually stop the ability of RNA & DNA polymerase involved in these processes to continue down the DNA strand.
E.g. Helicase will cause a twisting motion in the DNA strands.
Topoisomerase1: Break a phosphodiesterbond by nucleases without the use of ATP. Link it togheter later by ligases. Have a tyrosine in its active center. Reversable reaction.
Topoisomerase2: ATP-dependent. Break DNA on both strands
Name some common features for DNA polymerase
1: 5´-3´polymerase activity (read the strand 3-5direction)
2: Need primer to start (free 3´end hydroxyl)
3: Uses DNA a a template
4: dATP, dTTP, dCTP, dGTP
5: PPi product (pyrophosphate)
6: All DNA polymerase have 3-5exonuclease activity (proofreading). Type 1 have in addition, 5-3 exonuclease (removal of RNA primer)
DNA ligase function and requirements
The mechanism of DNA ligase is to form two covalent phosphodiester bonds between 3’ hydroxyl ends of one nucleotide, (“acceptor”) with the 5’ phosphate end of another (“donor”). ATP is required for the ligase reaction, which proceeds in three steps:
1: Adenylation (addition of AMP) of a lysine residue in the active center of the enzyme, pyrophosphate is released;
2: Transfer of the AMP to the 5’ phosphate of the so-called donor, formation of a pyrophosphate bond;
3: Formation of a phosphodiester bond between the 5’ phosphate of the donor and the 3’ hydroxyl of the acceptor. 3` attack this bond. AMP is a good leaving group.
Extra: Has lysine in its active center
What is a silent mutation?
Mutation in nonessential DNA
Cytosine can undergo spontaneous deamination to?
Uracil
This can make a mutation from C-G to A-T
Adenine and guanine can undergo deamination to?
Hypoxanthine and xantine, respectively
Nonsense mutation
Stop signal. AA sequence become shorter
Missense mutation
Code for different AA. Different protein is formed. Can be conservative or non-conservative
Frameshift mutation
Mutation caused by insertion or deletion of nucleotids. This shifts the triplet codon and alters many AA. Can make the protein longer or shorters
Epigenetics
Methylation on cytosine nucleotids. Shut off genes
Fatty acid metabolism: Lipoprotein lipase is stimulated by?
Insulin and Apoprotein C2 (which is transfered from HDL to VLDL and chylomicrons).
LPL break down TG to FA and glycerol
Does adipose tissue have glycerol kinase?
No. They need glucose (stimulated by insulin, GLUT4) to make glycerol 3-P.
What is the main difference between HMG-CoA in mitochondria and cytosol?
Cytosol: Cholesterol synthesis
Mitochondria: Ketone bodies synthesis
What is the first step in bile acid synthesis (which is also the rate-limiting)?
7a-hydroxylase
Inhibited by bile acids
HDL can give which lipoproteins to VLDL and chylomicrons?
ApoC2, ApoE
Cholesterol is converted to cholesterol ester by?
Lecithin:Cholesterol acyltransferase (LCAT) - In HDL?
Acyl:Cholesterol acyltransferase (ACAT) - For storage in cells
Function fo CEPT (cholesterol ester transfer protein)?
Exchange cholesterol ester with triglycerides. HDL can becomme TG rich
What is the difference between primary and secondary carnitine deficiency?
Primary: Inability to transport carnitine into the cells
Secondary: Caused by other metabolic disorders such as CAT2 Mutation, or Fatty acid oxidation disorders.
5´cap on mRNA consists of?
7-methylguanosine attached via a triphosphate
What makes up prokaryotic RNA polymerase?
2alpha, Beta for 5-3´polyemerase, Beta for template binding.
Togheter with the sigma factor (for the recognizion of the promoter) forms a holoenzyme
Consensus regions in prokaryotes
-35 and -10 (Pribnow box)
P-dependent and P-independent termination of RNA synthesis; what is the difference?
P-independent: RNA is self-complementary. RNA folds back on itsself forming a G-C righ stem plus a loop (hairpin). This facilitate the seoaration from the DNA-RNA hybrid helix. Palindromic , inverse repeat forms a hairpin loop and is believed to physically destabilize the DNA - RNA hybrid.
P-dependent: Require an additional protein, rho, which is a hexameric adenosine triphosphatase with helixase activity. Rho binds to a C-rich “rho recognition site” near the 5-end of the RNA strand until it reach the RNA polymerase paused at the termination site. The ATP dependent helixase separates the RNA-DNA hybrid helix, and release the RNA strand.
Consensus regions in eukaryotes
-25 (TATA or Hogness box), -80 (CAAT box)
TFIID recognize the promoter region
TFIIF binds the polymerase to to promoter
TFIIH has helixase activity
FU
What is splicing?
Removal of introns from exons. Occur in a spliceosome.
small nuclear RNA or snRNPs (snurps) are involved. U1-U6. snRNAs U1, U2, U4, U5 and U6 form complexes with 6-10 proteins each, forming small nuclear ribonucleoprotein particles (snRNPs).
After the formation of the full spliceosome, the U1 and the U4 snRNPs are detached and the remaining U2, U5 and U6 snRNAs are rearranged. This conformational change creates the catalytic spliceosome (transesterfication).
After the second transesterification reaction, the spliceosome comes apart. The snRNPs are recycled, and the spliced exons and the lariat intron are released.
What is the name of the enzyme which charge tRNA?
Aminoacyl-tRNA synthetase. Makes aminoacyl-tRNA. Need ATP -> AMP + PPi.
Two step reaction: Covalent attachment of a carboxyl of a amino acid to the 3-end of the tRNA.
Makes a 5`-aminoacyl adenylate intermediate
Aminoacyl-tRNA synthetase has proofreading
aa + tRNA + ATP -> Aminoacyl-tRNA + AMP + 2 Pi
Eukaryotic and prokaryotic ribosomes consists of two units. Which one?
Prokaryotic: 50S + 30S -> 70S
Eukaryotic: 60S + 40S -> 80S
Initiating of translation. Codon sequence and names
AUG sequence. AUG have N-formylated methione on bacteria and mitochondria. In eukaryotes, AUG code for methionine.
GUG codon can also initiate
SRP (signal recognition particle)
The signal recognition particle (SRP) is an abundant, cytosolic, universally conserved ribonucleoprotein (protein-RNA complex) that recognizes and targets specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes..
Its an ribozyme (RNA with enzymatic activity) and GTPase. (GTP for its dissociation). An RNAP complex containig an ancient RNA and six proteins RNA Uses GTP for its function
Which two AA is the only one coded by only one codon?
Methionine and tryphophan
What is the universal stop codons?
UAA, UAG, and UGA are stop codons and specify
the the end of translation of a polypeptide.
What is “Wobble base pair”?
A wobble base pair is a pairing between two nucleotides in RNA molecules that does not follow Watson-Crick base pair rules. The four main wobble base pairs are guanine-uracil (G-U), hypoxanthine-uracil (I-U), hypoxanthine-adenine (I-A), and hypoxanthine-cytosine (I-C)
Name of enzyme that transfer one AA to the growing polypeptide chain in ribosomes
Peptidyl transferase is an aminoacyltransferase
What is the Shine-Delgarno site?
The Shine-Dalgarno (SD) sequence is a ribosomal binding site in prokaryotic messenger RNA, generally located around 8 bases upstream of the start codon AUG. The RNA sequence helps recruit the ribosome to the messenger RNA (mRNA) to initiate protein synthesis by aligning the ribosome with the start codon.
Which Codons signals termination and how is it done?
Proteins known as “release factors” recognize the stop
codon (UGA, UAG, or UAA) at the A site. In E. coli RF-1 recognizes UAA and UAG, RF-2 recognizes UAA and UGA.
RF-3 binds GTP and enhances activities of RF-1 and –2.
Presence of release factors with a nonsense codon at A
site transforms the peptidyl transferase into a hydrolase,
which cleaves the peptidyl chain from the tRNA carrier.
Hydrolysis of GTP is required for disassociation of
RFs, ribosome subunit and new peptide.
Function of eIF2
eIF2 supplies Met-tRNA to 40S subunit. eIF2 phosphorylation inhibits initiation
Function of signal peptidases?
Signal peptidases are enzymes that convert secretory and some membrane proteins to their mature forms by cleaving their signal peptides from their N-terminals.
All signal peptidases described so far are serine proteases. The active site that endoproteolytically cleaves signal peptides from translocated precursor proteins is located at the extracytoplasmic site of the membrane. The eukaryotic signal peptidase is an integral membrane protein complex
Is the antisense or sense strand used for transcription?
Antisense (template)
Sense strand is the non-template
The direction of transcription on the different strands is opposite. This feature is referred to as asymmetric transcription.
Function of RNA polymerase
RNA polymerase catalyzes the formation of phosphodiesterase bonds between nucleotides (using triphosphate nucleotides)
Function of sigma factor
A sigma factor (σ factor) is a protein needed only for initiation of RNA synthesis. It is a bacterial transcription initiation factor that enables specific binding of RNA polymerase to gene promoters. As RNA polymerase elongate sigma factor looses its association with RNA polymerase. After 10-15 bp.
Name one inhibitor of RNA polymerase
1: α-Amanitin is an inhibitor of RNA polymerase II
2: Rifampicin: Important antibiotic. Rifampicin inhibits bacterial DNA-dependent RNA synthesis by inhibiting bacterial DNA-dependent RNA polymerase
3: actinomycin D. actinomycin D is shown to have the ability to inhibit transcription. Actinomycin D does this by binding DNA at the transcription initiation complex and preventing elongation of RNA chain by RNA polymerase
Function of cap binding proteins
Nuclear cap-binding protein complex is a RNA-binding protein which binds to the 5’ cap of pre-mRNA. The cap and nuclear cap-binding protein have many function in mRNA biogenesis including splicing, 3’-end formation by stabilizing the interaction of the 3’-end processing machinery, nuclear export and protection of the transcripts from nuclease degradation. When RNA is exported to the cytoplasm the nuclear cap-binding protein complex is replaced by cytoplasmic cap binding complex.
What is an lariat structure?
a ring of intron segments that has been spliced out of a messenger ribonucleic acid molecule by enzymes. Some introns form a long tail attached to the ring, giving the structure the appearance of a microscopic cowboy lariat.
What is the P-O ratio?
Definition: P/O ratio of oxidative phosphorylation
is the ATP produced per oxygen atom reduced by
the respiratory chain. 2,7 for NADH and 1,6 for FADH2.
Explanation: In mito chondria, for each two electrons transferred to ox ygen from NADH or FADH 2 , ten or six protons, respectively, are pum ped out of the matrix . The combination of the elec trogenic exchange of internal ATP for an external ADP by the ADP/ATP translocase and the non-elect rogenic symport of phosphate and a proton by the phosphate carr ier protein adds one proton to the total requir ed to provide ATP to the cellular cytoplasm, and so the bioenerget ic cost to the vertebrate mitochondrion is 3.7 protons . Therefore, the number of moles of ADP phosphoryl ated to ATP per two electrons transferred to oxygen, (P/O ratio), will be 10/3.7 and 6/3.7, or 2.7 and 1. 6 for NADH and FADH 2 , respectively.
Name one drug that inhibits electron transport chain
Oligomycin. Oligomycin A is an inhibitor of ATP synthase. In oxidative phosphorylation research, it is used to prevent state 3 (phosphorylating) respiration. Oligomycin A inhibits ATP synthase by blocking its proton channel (Fo subunit), which is necessary for oxidative phosphorylation of ADP to ATP (energy production)
Malonate is an competitive inhibitor of?
Succinate Dehydrogenase
Cyanide inhibits?
Complex 4 (Cytochrome c oxidase)
Lipid rafts consists of?
Cholesterol- and sphingolipid-enriched, highly dynamic, submicroscopic (25–100 nm diameter) assemblies, which float in the liquiddisordered lipid bilayer in cell membranes.
Function of DGAT (Diglyceride acyltransferase)
DGAT, catalyzes the formation of triglycerides from diacylglycerol and Acyl-CoA. The reaction catalyzed by DGAT is considered the terminal and only committed step in triglyceride synthesis and to be essential for the formation of adipose tissue.
Monoacyglycerol acyltransferases (MGATs)
Adaptins are important in?
Clathrin formation. Adaptins is the link between the cargo receptors and the clathrin. Formation of a polyhedral lattice
Adaptins are proteins that mediate the formation of vesicles by clathrin-coated pits, through interaction with membrane-bound receptors
Coat disassembly by hsc70 (ATPase)
Dynamin (a GTPase) pull the clathrin coated vesicle of the membrane.
Microtubles are made up of many?
Hetrodimers (alpha and beta tubulin). Connected with ATP they from filaments, with ADP they dissociate.
Difference between senscent and quiescent cell
Senescent cells: they have stopped dividing Quiescent cells: cell cycle is postponed until an appropriate signal (GF) is received
What is the steps in base-excision repair?
DNA glycosylase, AP-endonuclease, DNA polymerase 1 or E, DNA ligase
Steps in Nucleotide Excision Repair
Nucleotide excision repair (NER) is a particularly important excision mechanism that removes DNA damage induced by ultraviolet light (UV). UV DNA damage results in bulky DNA adducts - these adducts are mostly thymine dimers and 6,4-photoproducts. Recognition of the damage leads to removal of a short single-stranded DNA segment that contains the lesion. The undamaged single-stranded DNA remains and DNA polymerase uses it as a template to synthesize a short complementary sequence. Final ligation to complete NER and form a double stranded DNA is carried out by DNA ligase.
NER use UV-spesific endonucleases. UVRa, UVRb, UVRc and UVRd. Are involved. UVR = Ultraviolet light repair. The process of nucleotide excision repair is controlled in Escherichia coli by the UvrABC endonuclease enzyme complex, which consists of four Uvr proteins: UvrA, UvrB, UvrC, and DNA helicase II (sometimes also known as UvrD in this complex).
Xeroderma pigmentosum
In total, how many ATP is needed to add one amino acid to a growing polypeptide chain?
4 ATP/AA
Initiation of translation in prokaryotes need?
IF1, IF2, IF3
First 1+3, then 2 later on
IF-3 prevent 50S to bind
IF-2 bind to A-site and prevent other aminoacyl-tRNA to bind in the initiation phase.
Initiation of translation in eukaryotes
eIF4 bind to 5-cap of mRNA on 40S. Then, 40S try to find the first AUG sequence on mRNA (ATP-dependent).
Steps:
1: eIF3 + eIF1 bind to 40S.
2: eIF2 binds to P-site with tRNA (has GTP on it), eIF5b-GTP
3: eIF4 with mRNA finds AUG sequence
4: eIF5B hydrolyse eIF2 with GTP
5: initiation factors dissociate
Which part of the ribosome have peptidyltransferase activity?
23S
The elongation process in ribosomes need
GTP when ribosomes moves to the next codon
LAC operon: What is it and what does it code for?
Operon is a group of genes which are regulated and transcripted togheter. One promoter and one operon close to start side. Operon have one repressor. LAC operon contains genes for the transport and metabolism of lactose.
Activators: cAMP (inducer) -> Bind to CAP. Allow RNA polymerase to bind to promoter.
LAC repressor: allolactose
Genes: Lac Z, Lac Y and Lac A -> B-galoctisidase, lactose permease, galactoside O-acetyltransferase
What is desmolase and where can we find it?
Desmolase enzyme (20,22-desmolase): Oxidase. Inner MTM. NADPH + O2.
Rate-limiting!
Cholesterol side-chain cleavage enzyme, also called 20,22-desmolase; converts cholesterol to pregnenolone (+ isocaproaldehyde (C6))
What is StAr?
Sterogenic regulatory acute protein. Transport protein that regulates cholesterol transfer within the mitochondria, which is the rate-limiting step in the production of steroid hormones. It is primarily present in steroid-producing cells, including theca cells and luteal cells in the ovary, Leydig cells in the testis and cell types in the adrenal cortex.
Activators: cAMP (LH + ACTH). Angiotensin 2.
Name of inhibitor for mitotic spindle
colchicine
CYP11B1 and CYP11B2 is found where?
CYP11B2 in zona glomerulosa
CYP11B1 in zone fasiculata and reticularis
Aldosterone synthase consists of?
11-Hydroxylase (CYP11B1)
18-Hydroxylase (CYP11B2)
11-Dehydrogenase
Found in the mitochondrium
Androgen synthesis require both…
17-hydroxylase and 17,20 lyase
Signs of aldosterone excess and deficiency
Excess: Hypertension, hypokalemi, alkolosis
Deficiency: Loss of salt and water, hyperkalemi, acidosis
What is the function of 11beta-hydroxylase steroiddehydrogenase 2?
Convert cortisol to cortison (NAD+ dependent).
Cortisol, a glucocorticoid, binds the glucocorticoid receptor. However, because of its molecular similarity to aldosterone it is also capable of binding the mineralcorticoid receptor. Both aldosterone and cortisol have a similar affinity for the mineralocorticoid receptor; however, there is vastly more cortisol in circulation than aldosterone. To prevent over-stimulation of the mineralocorticoid receptor by cortisol, HSD-11β converts the biologically active cortisol to the inactive cortisone, which can no longer bind to the mineralocorticoid receptor. 11β-HSD co-localizes with intracellular adrenal steroid receptors. Licorice or Carbenoxolone, which contains glycyrrhetinic acid, can inhibit 11β-HSD and lead to a mineralocorticoid excess syndrome.
11bOHSDH2: Dehydrogenase - Cortisol inactivation, Cofactor: NAD+,
ER cytosolic surface
Epitelial MR target cells
11bOHSDH1: Reductase- Cortisol activation,
Cofactor: NADPH+H+,
ER luminal surface,
Liver, Adipose tissue, Lung
Name of disease and symtoms of excess cortisol
Cushing syndrome
Impaired glucose toleranse (DM) Central obesity Osteoporosis Muscle atrophy Stria Increased risk of infections
Name of disease and symtoms of cortisol dificiancy
Adrenal cortex insufficiency
Low BP, dehydration, K+ increase, Na+ decrease, impaired hari growth, exhaustion.
What is the problem with “Congenital adrenal hyperplasia”?
Partial or compleate deficiency of 21hydroxylase or 11betaHydroxylasen (CYP11B1)
No cortisol to suppress ACTH secretion: hyperplasia + production of excess androgens, starts in utero
ASAT and ALT need which cofactor?
PLP
What is the name of the enzyme which remove NH2 group from Glutamate? what does this enzyme need which cofactors? Regulation?
Glutamate dehydrogenase (GLUD). Need NAD+ or NADP+. This is a oxidative deamination reaction.
Activator: ADP + GDP
Inactivator: GTP + ATP + NH4+
GLUD1: Liver, kidney, other tissues
GLUD2: Brain + testies
What is the name of the two most common mechanism in humans to transport ammonia from the peripheral tissue to the liver?
Glutamine (by glutamine synthetase. Glutaminase in the liver). Glutamate + ATP + NH3 -> Glutamine + ADP + Pi
Alanine (alanine aminotransferase)
What is transdeamination?
Aminotransferase + Glutamate DH reaction
Reaction equation for the formation of carbamoyl phosphate. What is the regulations for this enzyme. Where does the second NH3 group come from?
Carbamoyl phosphate synthetase 1. In the mitochondria. Rate-limiting step. Free NH3 is formed by glutamate DH. Regulation: Activators -> N-acetylglutamate (this formation is stimulated by arginine).
NH3 + 2 ATP + CO2 -> Carbamoyl phosphate + 2ADP + Pi
The use of 2 ATP makes this reaction irreversable
Second NH3 from aspartate
Note: Carbamoyl phosphate synthetase 2 participates in the biosynthesis of pyrimidines.
List the enzymes in urea formation. How many enzymes do we have? How many ATP are needed per cycle?
1: Carbamoyl phosphate synthetase 1 (2ATP -> 2AMP + 2Pi)
2: Ornithine transcarbamoylase
3: Arginiosuccinate synthetase (ATP -> AMP + PPi)
4: Arginosuccinate lyase
5: Arginase
4 ATP/cycle
The two first enzyme reactions occur in the mitochondria
Overall stoichiometry: Aspartate + CO2 + 3ATP + NH3 + H2O -> Urea + AMP + 2 ADP + 2 Pi + 2 PPi + Fumarate
N-Acetylglutamate is formed by? Activator? What does this molecule stimulate
Acetyl-CoA + Glutamate by N-acetylglutamate synthetase
Activator: Arginine
Stimulate Carbamoyl phoshate synthetase 1
Asparagine synthetase and glutamine synthetase need?
ATP (Glutamate use 1 phosphate, Aspartate use 2 phosphates -> ATP -> AMP + PPi)
GS need free NH3
AS need glutamine as the NH3 donor
Which 7 intermediate does the carbon skeleton of amino acids form?
Pyrovate, Acetyl-CoA, Alpha-ketoglutatare, Oxaloacetate, Succinyl-CoA, Acetoacetate, Fumarate
Which Amino acid is the only exclusice ketogenic AA?
Leucine and lysine
