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

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