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Leucine Lysine
A. Classification of amino acid as exclusively glucogenic, glucogenic and ketogenic, or exclusively ketogenic
B.
Tryptophan Valine Histidine Arginine Leucine
Phenylalanine
PVT
Threonine
TIM
HALL
Lysine
Methionine
Isoleucine
Fig. 1 B. Some students may find PVT TIM HALL helpful in recalling the essential AA.
Functions of Proteins 1. Enzymatic catalysis 2. Transport and storage 3. Coordinated motion responsible for movements in the body (muscles) 4. Mechanical support support of body - bones and muscles 5. Generation and transmission of impulses 6. Control of growth and differentiation AA - simplest form of proteins 20 AA
Characteristics of proteins 1. Have more members 2. Fundamental component of protoplasm 3. Elements in protein C, H, O, N (I & Fe) 4. Proteins are considered macromolecules, composed of a number of AA joined together by peptide bond or linkage 5. Only foodstuff when absent in the diet will cause death 6. Utilize in the body for growth
Digestion of Proteins 1. Mouth - food is chewed 2. Stomach: Gastrin - triggers chief cells to release Hcl and pepsinogen 3. Small intestines: Secretin-stim. release of pancreatic juices Activation of proteolytic enzymes: Trypsinogen trypsin Chymotrypsinogen chymotrypsin Proelastase elastase Endo & exopeptidases activated
Products of enz action = amino acids Dipeptides & small peptides AA Greater amount of AA in portal blood is in the form of alanine
STOMACH Protein digestion starts in the stomach dietary proteins become denatured by gastric acid important for protein digestion because proteins are poor substrates for proteases ACID ENVIRONMENT is required for action of pepsin
PEPSIN A protease that works optimally at pH 2 a carboxyl protease acts mostly as endopeptidase does not cleave at random prefers peptide bonds formed by amino group of aromatic AA major breakdown products are not free AA but a mixture of oligopeptides known as peptones
INTESTINE As acidic stomach contents reach duodenum rapidly neutralized by HCO3 in pancreatic secretions. Proteolytic enzymes from pancreas include: 1. Trypsin a serine protease endopeptidase specific for CO side of basic AA
2. Chymotrypsin a serine protease endopeptidase specific for CO side of hydrophobic AA 1 & 2 = degrade peptones to smaller peptides 3. Carboxypeptidase A: hydrophobic AA at C terminal 4. Carboxypeptidase B basic AA at C terminus
PROTEIN TURNOVER A continuous process of protein degradation into AA and re-synthesis of proteins for AAs 1-2% of total body protein/day: primarily for degradation of muscle proteins RDA = 30 60 gm proteins/day PROTEIN QUALITY: Proportion of essential AA in food relative to their proportion in proteins being synthesized
excess AA are not stored those not incorporated into new proteins are rapidly degraded unlike CHOs and lipids, proteins and AA are not stored by the body proteins are present in all cells some of the bodys proteins can be mobilized during fasting or starvation C skeletons of AAs are burned for energy or converted to glycogen or TG stored.
Amino acid pool: is not a storage place for AAs is a convenient way to indicate that small amounts of AAs are present in cells or circulate in blood During starvation: much of plasma proteins (esp albumin) are utilized first rapidly metabolizing tissues (liver, pancr, intesti mucosa) - tend to lose their proteins quickly muscle is slow to yield AAs
MAJOR PATHWAYS FOR DEGRADATION OF INTRACELLULAR PROTEINS 1. Lysosomal membrane-associated proteins long-lived intracellular proteins cathepsins 2. Cytosolic require ubiquitin, ATP for abnormal and short-lived proteins
WHAT FACTORS TARGET A PROTEIN FOR DEGRADATION? For proteins in circulation: loss of sialic acid moiety from non-reducing ends of oligosaccharide chains signal degradation asialated glycroproteins recognized by receptors in liver cells internalized degraded in lysosomes by cathepsins
THE 20 AMINO ACIDS USED FOR BUILDING PROTEIN CHAINS: Aliphatic nonpolar side chains: gly leu val ala ile Aromatic side chains: phe tyr trp Hydroxyl-containing side chains: ser thr
Acidic side chains: asp (d) glu (e) Amidic amino acids: asn (n) gln (q) Basic side chains: lys arg his Sulfur-containing side chains: cys met Imino acid: pro
Common AAs = those AAs for which at least one specific codon exists in the genetic code Derived AAs = in proteins are formed from one of the common AAs after the common AA has been incorporated into protein structure Aromatic AAs: Phe contains benzene ring Tyr contains phenol grp Trp = R grp contains a heterocyclic structure indole nucleus * In all 3 AAs the aromatic moiety is attached to the a-c thru a methylene (-CH2)
CONVERSION OF AMINO ACIDS TO SPECIALIZED PRODUCTS 1. Glycine a. A-carbon & N atom used for synthesis of porphyrin moiety of Hb b. Entire gly mol forms position 4,5,7 of purine skeleton c. gly + cholic acid glycocholic acid (bile acids) d. gly + sam sarcosine (n-methyl-gly) component of creatine
2. Alanine Ala + gly amino N2 in human plasma -ala + his present in carnosine
(major % in humans) (skel musc dipeptide)
3. Arginine - formamidine donor for creatine synthesis in primates 4. Ornithine a. plays a role in urea biosynthesis b. precursor or mammalian polyamines spermidine & spermine
6. Tyrosine precursor of epinephrine & norepinephrine precursor of thyroid hormones - triiodothyronine (T3) & thyroxine (T4) 7. Creatine & Creatinine Creatine - present in muscle, brain, blood as phosphocreatine free creatine nly present in urine (traces) synthesis involves 3 AAs gly, arg, met
8. Gaba - -aminobutyrate formed fr glutamate by decarboxylation catabolism involves transamination succinate semi-aldehyde succinate
Amino Acid Precursor Ser, met Tyr Tyr, met Trp Glu His Ornithine met Arg, gly, met
Distinguishing Features of Pathways Sam is methylating agent L-dopa is intermediate & precursor of melanins Sam-dependent transaminase activated by glucocorticoids 5-hydroxy trp is intermediate (5-HT) Decarboxylation reaction Decarboxylation reaction Spermidine is intermediate Guanidino grp transferred to gly
ESSENTIAL AND NONESSENTIAL AMINO ACIDS Essential Methionine Arginine Phenylalanine Threonine Valine Tryptophan Histidine Isoleucine Leucine Lysine Nonessential Glutamate Glutamine Proline Aspartate Asparagine Alanine Glycine Serine Tyrosine Cysteine