Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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