Biochemistry: Protein and Nucleotide Metabolism

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Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

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