Science Quiz / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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