Products from Amino Acids
Name at least three compounds derived from glycine.
Protoporphyrin IX (heme), purines, glutathione (amino acid uptake), bile salts.
List all of the amino acids that serve as precursors for creatine and discuss its function.
Glycine, methionine, arginine. Creatine stores phosphate as creatine phosphate; can combine with ADP when energy needed.
Discuss the value of urinary creatinine measurements by clinical chemists.
Creatinine is decomposed into creatinine. Excretion is constant over 24 hr. period. Normal values = 0.7-1.5 mg/dL. 2-4 mg/dL suggests renal failure.
Name molecules derived from serine.
Sphingosine & its derivatives, phosphatidyl serine, cysteine.
Name molecules derived from tryptophan.
Name molecules derived from Methionine.
S-Adenosylmethionine, creatine phosphate, choline.
Recognize the structure of ornithine and name two molecules that are derived from it.
Citrulline and polyamines (spermidine/spermine). Strucuture is drawn in notes.
Name the amino acid used to form the structure of thyroid hormone and the element that is a part of this hormone that is not commonly found in biological molecules.
Tyrosine; contains iodine.
Name and recognize the molecule that most commonly serves as the donor of methyl groups in biological methylation reactions.
Recognize the structures of spermine and spermidine. Indicate the parts of these molecules that are derived from methionine (decarboxySAM) and from ornithine.
Spermidine: left is ornithine, right is decarboxySAM
Spermine is same as spermidine, except another decarboxySAM unit is added to right. (see notes)
Discuss the biological functions of histamine.
Neurotransmitter in brain, local mediator. H1 receptor- sleep-wake cycles (activate PLC). H2 receptor- stomach acid production.
List the major sites of carnitine synthesis.
Liver and kidney.
Name the molecule that is used as the precursor for carnitine and list the cofactors required for carnitine synthesis.
Trimethyllysine is precursor for carnitine; reaction requires NAD+, Vitamin C, Fe2+ to keep hydroxylases active.