Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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