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

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