Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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