Biochem - E4 Flashcards
Aa –> acetyl coA
Leucine, lysine
Phenylalanine, tyrosine, tryptophan
Aa –> pyruvate
alanine, cysteine, glycine, serine, threonine
Aa –> oxaloacetate
asparagine –> aspartate –> oxaloacetate.
Aa –> fumerate
aspartate, phenylalanine, tyrosine
Aa –> succinyl CoA
Isoleucine, methionine, threonine, valine
Aa –> fumarate and acetoacetate
Phenylalanine, tyrosine
Branched amino acid breakdown
The Breakdown of Branched Chain Amino Acids (Valine, Isoleucine, Leucine) is via aminotransfer to form keto acids, and then the action of a BCAA dehydrogenase
Defective dehydrogenase –> maple syrup urine disease
- muscle prefers branched, liver has NO branched-chain aminotransferase
Periportal region of liver
Converts ammonia to urea
Perivenous region of liver
Converts ammonia to glutamine
Some glycogenic amino acids are interconvert with a-Ketoglutarate (via glutamic gamma-semialdehyde)
Arginine *and ornithine Proline Glutamine Glutamate --> alpha-ketoglutarate
Propionyl-CoA –> succinyl-CoA requires
biotin and vitamin B12
methylmalonate buildup –> dx of
methylmalonyl CoA MUTASE defect (due to lack of vitamin B12, or prob w/ absorption w/ intrinsic factor, or prob with conversion to adenosyl form of vitamin B12)
Adenosylcobalamine
Vitamin B12 in the adenosyl form –> needed for catabolism of valine, isoleucine, methionine. (all go to propionyl CoA –> succinyl CoA)
Vitamin form would be -OH or -CN
Oxaloacetate pathway
Asparagine –> aspartate –> oxaloacetate ( –> PEP –> glucose)
Phenylalanine –> tyrosine rxn
Via phenylalanine hydroxylase and tetrahydrobiopterin
dihydrobiopterin –> tetrahydrobiopterin
dihydrobiopterin reductase
PKU is due to which deficiency
Via phenylalanine hydroxylase deficiency OR due to dihydrobiopterin reductase deficiency
Which aa makes nitric oxide
arginine * an essential aa
Tyrosine –> dopa
Via tyrosine hydroxylase and tetrahydrobiopterin
Tyrosine –> Dopa —?—> dopamine
Via decarboxylase and PLP
? –> thyroxine (T4)
Tyrosine + iodine (on thyroglobulin protein) –> thyroxine (thyroid peroxidase)
? –> melanin
tyrosine –> melanin. Via tyrosinase (tyrosine-3-monooxygenase)
Albinism
tyrosine –> melanin. Via tyrosinase (tyrosine-3-monooxygenase) (defective –> albinism)
Rxns requiring PLP (pyrodoxial phosphate)
Aminotransferase rxn –> exchange between keto/amino forms of aa
THF + serine –> glycine + methylene form THF
Dopa –> Dopamine
Homocysteine –> cystathione (–> cysteine)
Gout
Increased uric acid in blood
Deficiency in HGPRT, or PRPP synthase, or G-6-Pase deficiency (increased PPS, xs R-5-P)
Tx for gout
Allipurinol
^ hypoxanthine analogue, competitive inhibitor of xanthine oxidase.
hypoxanthine and xanthine accumulate –> more soluble than uric acid
Lesch-Nyhan Syndrome
lack functional HGPRT (increased uric acid in serum)
- -> self-mutilation, mental illness and gout like sx
- Marked increase in the rate of purine biosynthesis by the de novo pathway
SCID
ADA (adenosine deaminase deficiency)
Sulfonamides
Antibacterial agents. Resemble p-aminobenzoic acid and inhibit synthesis of folate in bacteria, thus unable to form purines and thus their duplication is blocked. Humans not affected by sulfonamides (bc dietary folate).
6-mercaptopurine
analogue of hypoxanthine, rely on activation by salvage pathway
After salvage, a potent competitive inhibitor of IMP in the pathways for AMP and GMP biosynthesis.
Once combined with PRPP it acts as a competitive inhibitor of IMP in the pathways for AMP and GMP biosynthesis.
Tx for acute leukemia
Gastric glands
secrete Hcl and pepsinogen
Pepsinogen
propeptide of pepsin binds at high pH (inside cells, for example)
Pepsin –> active at low pH
Pancreas
Secretes bicarbonate & neutralizes stomach contents (pH increases to 7 in duodenum) Secretes zymogens (trypsinogen, chymotrypsinogen, proelastase, procarboxypeptidase) through pancreatic duct
CCK
secreted by cells in the duodenum and stimulates the release of bile into the intestine and the secretion of enzymes by the pancreas.