| Clue | Answer |
|---|
| Lacking OMP decarboxylase or orotate phosphoribosyltransferase causes this rare metabolic condition. Patients often have aneamia, leukopenia and retarded development. | |
| This enzyme converts hypoxanthine to xanthine | |
| Deficient enzyme in maple syrup urine disease | |
| Creatine phosphate 'buffers' ___________ during exercise so it doesn't significantly drop. | |
| HGPRT ___________________ causes an increase in the rate of purine synthesis. (Deficiency/Hyperactivity) | |
| This enzyme combines ornithine and carbamoyl phosphate to make citrulline | |
| This enzyme converts Carbamoyl aspartate to Dihydroorotate | |
| This isoform of CK is found in the heart and is important in diagnosing MIs. | |
| What product builds up in ADA deficient SCID that inhibits deoxynucleotide synthesis | |
| Ribose-5-Phostphate is an intermediary in what pathway? | |
| A genetic mutation leading to a deficiency in HGPRT leads to what condition? | |
| A deposit of urate crystals in someone with gout | |
| This enzyme converts dihydrofolate to tetrahydrofolate | |
| One type of this autosomal recessive disease stems from a deficiency of phenylalanine hydroxylase | |
| Condition when uric acid crystals precipitate out of the blood | |
| What type of amino acids are not principally oxidized in the liver? | |
| This is the first enzyme to rise following a myocardial infarction and may only rise transiently and normalize in less thatn 3 days. | |
| What is molecule is 'activated ribose'? | |
| This isoform of creatine kinase is found in smooth muscle and brain tissue and makes up only 1% of total CK. | |
| CTP Synthase aminates UTP with an amino group from where? | |
| This enzyme found in the gut cleaves urea to get carbon dioxide and ammonia. | |
| Segments rich in what amino acids are rapidly degraded? (acronym) | |
| What amino acid donates an amino group to PRPP? | |
| Coverts dihydroorotate to orotate with FAD | |
| This enzyme is deficient in albinism. | |
| What amino acid is added to IMP to make AMP? | |
| What is the product of the rate limiting step of the urea cycle | |
| This amino acid has two amino groups and is thus the most efficient carrier of ammonia | |
| 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. | |
| What type of reaction can create non-essential amino acids from essential amino acids or non-essential AAs from non-essential AAs. | |
| This amino acid is used in the production of melanin | |
| This disease causes increased levels of histidine in the blood and urine and causes mental retardation | |
| This isoform of creatine kinase is in skeletal muscle and makes up 95% of the CK in the body. | |
| This metabolite inhibites ribonucleotide reductase leading to the inability of cells to synthesize deoxyribonucleotides and therefore DNA. | |
| Since humans can't store purines we must get rid of them in this form | |
| During periods of malnutrition, starvation, cachexia and after traumatic injury the nitrogen balance is _________________. | |
| Deamination reactions create this highly toxic chemical that must be removed from the body. | |
| This molecule inhibits CPS-II | |
| 20% of SCID cases are due to this enzyme deficiency | |
| This enzyme phosphorylates CPS-II to change its allosteric properties making it more easily inhibited | |
| Aspartate, Arginine, Leucine, Lysine and Phenylalanine are which type of N-Terminal amino acids? | |
| A muscle cell that is fully charged with CP has a __________:1 ratio of CP:ATP | |
| This enzyme catalyzes the conversion of bicarbonate and ammonia (from glutamine) to carbomoyl phosphate, releasing glutamate. | |
| This is a common cause of acquired hyperammonemia. | |
| This enzyme can convert Adenosine to Inosine | |
| This enzyme catalyzes the formation of IMP and GMP from Hypoxanthine and Guanine and PRPP | |
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