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