Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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