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26 Cards in this Set
- Front
- Back
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Amino Acids necessary for purine synthesis |
GAG, Glycine, Aspartate, Glutamine. |
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Leflunomide inhibits |
dihydroorotate dehydrogenase |
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Mycophenolate and ribavirin inhibit |
IMP dehydrogenase |
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Hydroxyurea inhibits |
Ribonucleotide reductase |
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6MP and its prodrug azathioprine inhibit |
de novo purine synthesis |
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5-FU inhibits |
thymidylate synthase (decreases dTMP) |
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Methotrexate (MXT), Trimethoprim (TMP), and pyrimethamine inhibit |
dihydrofolate reductase (decreases dMTP) in humans, bacteria, and protozoa respectively |
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Lesch-Nyhan syndrome |
Defective purine salvage due to absent HGPRT; Hyperuricemia Gout Pissed off (aggression, self-mutilation) Retardation (intellectual disability) DysTonia |
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He's got purine recovery trouble |
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Adenosine deaminase deficiency |
One of the major causes of autosomal recessive SCID.
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Allopurinol |
Inhibits XO inhibiting uric acid formation |
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Example of missense mutation |
Sickle cell disease |
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Example of Frameshift mutations |
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Nucleotide excision repair |
Xeroderma pigmentosum |
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Mismatch repair |
Defective in hereditary nonpolyposis colorectal cancer (HNPCC) |
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Nonhomologus end joining |
Mutated in ataxia telangiectasia |
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mRNA start codons |
AUG (or rarely GUC) AUG inAUGurates protein synthesis |
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mRNA stop codons |
UGA = U Go Away UAA = U Are Away UAG = U Are Gone |
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Helicase |
Unwinds DNA template at replication fork |
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Single-stranded binding proteins |
Prevent strands from reannealing |
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DNA topoisomerases |
Create a single or double stranded break in the helix to add or remove supercoils |
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Primase |
Makes an RNA primer on which DNA polymerase III can initiate replication |
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DNA polymerase III |
Prokaryotic only. |
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DNA polymerase I |
Prokaryotic only. Degrades RNA primer; replaces it with DNA |
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DNA ligase |
Catalyzes the formation of a phosphodiester bond with a strand of double-stranded DNA (i.e. joins Okazaki fragments) |
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Telomerase |
An RNA-dependent DNA polymerase that adds DNA to 3' ends of chromosomes to avoid loss of genetic material with every duplication. |
