Science Quiz / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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