Science Quiz / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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Created Dec 17, 2012ReportNominate
Tags:biochemistry, nucleotide, protein

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