Science / Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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