Term
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Definition
| (Stomach) Stimulates gastric HCl secretion |
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Term
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Definition
| (small intestine) stimulates bicarbonate secretion to neutralize the gastric HCl and increase the pH to about 7 |
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Term
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Definition
| (small intestine) promotes secretion of several pancreatic enzymes with optimal activity at pH 7 to 8 |
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Term
| What are the two steps of amino acid degradation |
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Definition
- Step 1: Removal of the amino-group (transferthe amino group to alpha-ketoglutarate to form L-glutamate)
- PLP functions as an intermediate carrier of amino groups on the active site of transaminases
- Step 2: Breakdown of the carbon skeleton
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Term
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Definition
| Alanine + α-Ketoglutarate ⇄ Pyruvate + Glutamate |
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Term
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Definition
| L-Leucine + α-Ketoglutarate ⇄ α-Ketoisocaproate + L-Glutamate |
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Term
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Definition
| Tyrosine + α-Ketoglutarate ⇄ p-Hydroxyphenylpyruvate + Glutamate |
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Term
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Definition
Deamination is a means of amino acid degradation that predominatly occurs in the liver. It entails the loss of an amino (-NH2) group that is used to produce ammonia
The α-amino groups of serine and threonine can be directly deaminated because each of these amino acids contains a hydroxyl group in its side chain. These direct deaminations are catalyzed by serine dehydratase and threonine dehydratase, which
PLP is the prosthetic group.
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Term
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Definition
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Term
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Definition
| Threonine → α-Ketobutyrate + NH4+ |
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Term
| Amino Acids that are degraded to pyruvate |
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Definition
6 amino acids SGT WAC likes Pye - Serine (S)
- Glycine (G)
- Threonine (T)
- Tryptophan (W)
- Alanine (A)
- Cysteine (C)
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Term
| Amino Acids that are degraded to Acetyl-CoA |
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Definition
7 amino acids Ace, FLY WIT K - Phenyalanine (F)
- Tyrosine (Y)
- Leucine (L)
- Tryptophan (W)
- Isoleucine (I)
- Threonine (T)
- Lysine (K)
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Term
| Amino acids that are converted to alpha-ketoglutarate |
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Definition
5 amino acids KATE knows her P's and Q's - Histidine (H)
- Glutamate (E)
- Arginine (R)
- Proline (P)
- Glutamine (Q)
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Term
| Amino acids that are converted to Succinyl-CoA |
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Definition
4 Amino Acids I just "Met" "Val" and told her to Succ I.T. - Methionine (M) (Met)
- Valine (V) (Val)
- Isoleucine (I)
- Threonine (T)
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Term
| Amino Acids that are converted to oxaloacetate |
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Definition
2 amino acids - Asparagine (N)
- Aspartic acid (D)
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Term
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Definition
| The amino acids degraded to pyruvate, a-ketoglutarate, succinyl-CoA, fumarate, and/or oxaloacetate can be converted to glucose and glycogen Alanine, Arginine, Asparagine, Aspartic acid, Cysteine, Glutamic acid, Glutamine, Glycine, Histidine, Isoleucine, Methionine, Proline, Serine, Threonine, Tryptophan, Valine, Phenylalanine, and Tyrosine. |
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Term
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Definition
The amino acids degraded entirely or in part to acetoacetyl-CoA and/or acetyl-CoA, can yield ketone bodies in the live. Leucine, Lysine, Threonine, Tryptophan, Isoleucine, Tyrosine, and Phenylalanine |
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Term
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Definition
W.I.F.T.Y.
Amino acids that haveboth activities Phenylalanine (F), Tyrosine (Y), Tryptophan (W), Threonine (T), and Isoleucine (I)
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Term
| Where does the first amino group to enter the urea cycle come from |
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Definition
| The first amino group to enter the urea cycle arises in the form of free ammonia by the deamination of glutamate inside the mitochondria of the liver cells. |
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Term
| Carbamoyl Phosphate Synthetase I |
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Definition
- catalyzes the formation of carbamoyl phosphate
- free ammonia is immediately used together with carbon dioxide generated in the mitochondria by respiration, to form carbamoyl phosphate in the matrix in an ATP-dependent reactio
- terminal phosphate groups of two molecules of ATP are used to form one molecule of carbamoyl phosphate
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Term
| Ornithine Transcarbamoylase |
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Definition
- Carbamoyl phosphate donates its carbamoyl group to ornithine to form citrulline and releases its phosphate.
- a Mg2+ requiring mitochondrial enzyme
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Term
| Where does the second amino group come from? |
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Definition
- the second amino group is introduced in the form of L-aspartate formed from oxaloacetate + L-glutamate via Aspartate transaminase
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Term
| Argininosuccinate Synthetase |
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Definition
- The transfer of the second amino group to citrulline occurs by a condensation reaction between the amino group of aspartate and the carbonyl carbon of citrulline in the presence of ATP to argininosuccinate.
- Argininosuccinate synthetase is a Mg2+ dependent enzyme
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Term
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Definition
- cleaves argininosuccinate into arginine and fumarate
- note that the carbon skeleton of aspartate is preserved in these reactions, which transfers the amino group of aspartate from arginine
- fumarate returns to the pool of Citric Acid Cycle intermediates.
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Term
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Definition
- cleaves arginine to yield urea and ornithine
- ornithine can then enter the mitochondria again to initiate another round of the urea cycle
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Term
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Definition
The treatment of urea cycle disorder consists of balancing dietary protein intake so that the body receives the essential amino acids responsible for cell growth and development, but not too much protein from which excessive ammonia is formed. Example 1: Supplementing the diet with arginine is useful in treating deficiency of ornithine transcarbamoylase, argininosuccinate synthetase, and argininosuccinase. Example 2: In the case of arginase deficiency, arginine, the substrate of the defective enzyme, must be excluded from the diet. |
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Term
| Non-Essential Amino Acids |
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Definition
Getting the DEANS list is not essential
- Aspartate (D)
- Glutamate (E)
- Alanaine (A)
- Asparagine (N)
- Serine (S)
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Term
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Definition
- Arginine
- Cysteine
- Glutamine
- Glycine
- Proline
- Tyrosine
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Term
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Definition
MILK WTH Vagina and Fellatio are Essential
- Methionine (M)
- Isoleucine (I)
- Leucine (L)
- Lysine (K)
- Tryptophan (W)
- Threonine (T)
- Histidine (H)
- Valine (V)
- Phenylalanine (F)
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Term
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Definition
- active form: Pepsin
- converted bypepsin
- works in the Stomach
- Amino Acid: Tyr, Phe, Trp
- Cleaves he amino-terminal side
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Term
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Definition
- active form:Trypsin
- converted by enteropeptidase
- works in the small intestine
- Amino Acid: Lys, Arg
- Cleaves the carboxyl group
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Term
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Definition
- active form: Chymotrypsin
- converted by trypsin
- works in the small intestine
- Amino Acid: Tyr, Phe, Trp
- cleaves at the carboxyl group
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Term
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Definition
- action site: small intestine
- Amino acid or peptide: carboxyterminal residues
- cleavage point: it cleaves the peptide bond nearest to the terminal carbonyl group in polypeptide chains
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Term
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Definition
- action site: small intestine
- amino acid or peptide: basic amino acids lys, arg, and ornithine
- Cleavage point: it catalyzes hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position in polypeptides
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Term
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Definition
- action site: small intestine
- Amino Acid or peptide: amino terminal residues (exept proline)
- Cleavage Point: any of various enzymes that catalyze the hydrolysis of the terminal peptide bond at the amino end of a polypeptide
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