Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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