Science Quiz / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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ClueAnswer
Elimination of an amino group
Increased BUN usually indicates ________________ disease.
Since humans can't store purines we must get rid of them in this form
A deficiency of this enzyme would be indicated by Argininosuccinic Acidemia
A deficiency of this enzyme would be indicated by Argininemia
This enzyme converts hypoxanthine to xanthine
What is the base in IMP?
Enzyme that transaminates alanine
What amino acid donates an amino group to PRPP?
________________ cause poor myelination and mental retardation.
Glycine, arginine and methionine are used to synthesize what?
What amino acid is added to IMP to make GMP?
This genetic disease is characterized by self-mutilating behavior
GMP, GDP, GTP, AMP, ADP and ATP all inhibit what enzyme?
A deposit of urate crystals in someone with gout
This enzyme removes an ammonium ion from glutamate to make alpha-ketoglutarate.
Ribose-5-Phostphate is an intermediary in what pathway?
This enzyme converts 5-phosphoribosyl-1-pyrophosphate to 5-phosphoribosyl-1-amine
What immune cell carries out de novo synthesis of nucleotides?
Deficiency of this enzyme would lead to increased levels of orotic acid
A polymer of this chemical creates a black-brown pigment that deposits in connective tissue and can be seen in standing urine in people with alkoptonuria.
Creatine kinase is only made in muscle cells that are _________________.
Lacking OMP decarboxylase or orotate phosphoribosyltransferase causes this rare metabolic condition. Patients often have aneamia, leukopenia and retarded development.
This enzyme is deficient in histidinemia
Ezyme that transaminates aspartate
This amino acid has two amino groups and is thus the most efficient carrier of ammonia
Enzyme that converts dUMP to dMP
This isoform of creatine kinase is in skeletal muscle and makes up 95% of the CK in the body.
Bicarbonate, aspartate and ammonia are used to make what?
This enzyme converts Carbamoyl aspartate to Dihydroorotate
In PKU which amino acid becomes essential?
What immune cell uses primarily the salvage pathway for nucleotide synthesis?
Aminotransferase put the amino group from alanine on alpha-ketoglutarate to form glutamate and ___________________.
Deficient enzyme in maple syrup urine disease
This enzyme can convert Adenosine to Inosine
This disease causes increased levels of histidine in the blood and urine and causes mental retardation
________________ have a maple/cheesy smell.
This enzyme is deficient in albinism.
During periods of growth, pregnancy and convalescence the nitrogen balance is _________________.
This amino acid is used in the production of melanin
The methyl group needed for the conversion of dUMP to dTMP comes from...
Coverts dihydroorotate to orotate with FAD
This enzyme combines citrulline and aspartate to argininosuccinate
Pyrophosphates are the basis of this drug class which is used to treat osteoporosis.
What amino acid is added to IMP to make AMP?
Decreased BUN usually indicates ______________ disease.
CPS-II is most sensitive to PRPP during what cell phase?
ClueAnswer
The glycine residue at the carboxyl end of ubiquitin attaches to what residue on the target protein?
20% of SCID cases are due to this enzyme deficiency
The deficient enzyme in alkaptonuria breaks down tyrosine to form _____________.
This enzyme found in the gut cleaves urea to get carbon dioxide and ammonia.
This type of base is sythesized piece by piece directly on the ribose
Converts OMP to UMP
CPS-II is most sensitive to UTP during the end of which cell phase?
This enzyme converts Xanthine to Uric Acid
The most commonly inherited urea enzyme deficiency
Ketogenic amino acids yield which compound(s)?
This enzyme converts UTP to CTP
How is maple syrup urine disease treated?
This molecule inhibits CPS-II
Creatine phosphate 'buffers' ___________ during exercise so it doesn't significantly drop.
Branched chain ketoacid dehydrogenase requires what cofactor?
What enzyme synthesizes PRPP?
Homocystein and methionine levels are increased in this disease that causes mental retardation and dislocation of the lens of the eye.
This drug binds to glutamine and is then excreted from the body in order to reduce the ammonia in the body
Phenylpyruvate and phenylacetate are _____________.
Cofactor of all aminotransferase reactions because amino group is first transferred to this molecule.
Enzyme that converts thymidine to TMP
This enzyme converts Argininosuccinate to Arginine and Fumarate.
Segments rich in what amino acids are rapidly degraded? (acronym)
Enzyme that converts THF to N5, N10-methylene THF
This enzyme converts dihydrofolate to tetrahydrofolate
This molecule allosterically activates CPS-I
This enzyme phosphorylates CPS-II to change its allosteric properties making it more easily activated
This enzyme converts neucleotides to nucleosides
In a healthy person ketovaline is broken down into ______________>
What enzyme is deficient in alkaptonuria?
This enzyme adds an ammonium ion to glutamate to make glutamine
This metabolite inhibites ribonucleotide reductase leading to the inability of cells to synthesize deoxyribonucleotides and therefore DNA.
This molecule inhibits thymidine kinase
This enzyme catalyzes formation of AMP from adenine and PRPP
PRPP synthase is negatively regulated by ________________
What substrate is used to synthesize PRPP?
What are uric acid crystals interacting with in gouty arthritis?
Treatment for Lesch-Nyhan Sydrome?
This enzyme converts carbomoyl phosphate to carbomoyl aspartate
Aspartate, Arginine, Leucine, Lysine and Phenylalanine are which type of N-Terminal amino acids?
Deamination reactions create this highly toxic chemical that must be removed from the body.
What molecule is at the branch point of de novo purine synthesis?
Enzyme that converts deoyuridine to dUMP
Homocystinuria results from a deficiency of this enzyme
With what disease would a patient have high levels of valine, leucine and isoleucine in their blood?
A muscle cell that is fully charged with CP has a __________:1 ratio of CP:ATP
Purine nucleosides are converted to free bases by what enzyme?
ClueAnswer
What amino acids are purely ketogenic?
Alanine, glycine, methionine, serine, threonine and valine are which type of N-terminal residues?
Deamination occurs primarily on this amino acid because it is the end produce of many transamination reactions.
This transaminase enzyme helps the urea cycle by being involved in the recycling of fumarate to aspartate.
A genetic mutation in what enzyme can cause increased de novo synthesis of purines and hyperuricemia
This small, basic protein tags proteins for degradation
A genetic mutation leading to a deficiency in HGPRT leads to what condition?
Converts orotate to OMP
What type of amino acids are not principally oxidized in the liver?
In hereditary hyperammonemia the administration or citrulline and arginine is usually effective except in the case of _______________.
What enzyme converts ribonucleotides to deoxyribonucleotides
What product builds up in ADA deficient SCID that inhibits deoxynucleotide synthesis
This enzyme catalyzes the conversion of bicarbonate and ammonia (from glutamine) to carbomoyl phosphate, releasing glutamate.
HGPRT ___________________ causes an increase in the rate of purine synthesis. (Deficiency/Hyperactivity)
Condition when uric acid crystals precipitate out of the blood
People with hyperammonemia are given ________________ so the body uses it for energy of protein
This drug binds to glycine in the liver and is excreted in order to reduce ammonia in the body.
Presence of creatine kinase in the blood can indicate ___________________.
Lysosomal degradation activity is ______________ during starvation? (Increased/Decreased)
The most effective treatment for SCID
Transfer of an amino group from one amino acid to an amino acid carbon skeleton or alpha ketoacid.
A deficiency of this enzyme would be indicated by citrullinemia.
A very high protein diet or starvation would lead to __________________ (induction/repression) of urea cycle enzymes.
One type of this autosomal recessive disease stems from a deficiency of phenylalanine hydroxylase
This isoform of CK is found in the heart and is important in diagnosing MIs.
This enzyme phosphorylates CPS-II to change its allosteric properties making it more easily inhibited
Normal BUN:Creatinine level is ____________:1
During periods of malnutrition, starvation, cachexia and after traumatic injury the nitrogen balance is _________________.
This molecule activtivates CPS-II
This is the first enzyme to rise following a myocardial infarction and may only rise transiently and normalize in less thatn 3 days.
What is the product of the rate limiting step of the urea cycle
Creatine phosphate donates its phosphate group to ADP after _________________.
This single bifunctional enzyme has the properties of orotate phosphotranfserase and OMP decaboxylase
This is a common cause of acquired hyperammonemia.
This isoform of creatine kinase is found in smooth muscle and brain tissue and makes up only 1% of total CK.
CTP Synthase aminates UTP with an amino group from where?
If the CK found in the heart is greater than ______ U/L then an MI is probable.
The commited step of de novo purine synthesis is conversion of PRPP to ____________________.
This type of base is assembled completely first then attached to a ribose
What type of reaction can create non-essential amino acids from essential amino acids or non-essential AAs from non-essential AAs.
The cofactor required for transamination reaction is a derivative of ______________.
This enzyme converts creatine to creatine phosphate.
This enzyme combines ornithine and carbamoyl phosphate to make citrulline
Most de novo nucleotide synthesis occurs where?
Lysosomal proteases that degrade protein in the lysosomal pathway
This enzyme catalyzes the formation of IMP and GMP from Hypoxanthine and Guanine and PRPP
What is molecule is 'activated ribose'?

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