Science Quiz / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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