Can you name the Biochemistry: Protein and Nucleotide Metabolism?

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

  1. by athomps33
  • Created Dec 17, 2012 in Science
  • Game Plays 25

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