Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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