Amino Acids And Proteins

Front 1

Catalyze almost all reactions in living cells

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Protein

Front 2

Each amino acid is linked by

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Peptide bond

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End of protein structure with a free amino group

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N-Terminal

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End of protein structure with a free carboxyl group

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C terminal

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Where N and C terminal bond to form peptide bond

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Alpha carbon

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Protein acceptor

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Amino group

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Protein donor

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Carboxylic acid group

Front 8

Protelytic enzymes to completely digest dietary proteins

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Hydrochloric Acid

Trypsin

Pepsin

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Amino group is removed by

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deamination or transamination

Front 10

Can enter into a metabolic pathway with carbohydrates and fats

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Resultant ketoacid

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Generates precursors of glucose such as pyruvate or Citric Acid Intermediate

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Glucogenic Amino Acid

Front 12

Generate ketone bodies

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Ketogenic amino acid

Front 13

Essential amino acid required for Generation of Urea and synthesis of creatinine

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Arginine

Front 14

Essential amino acid that maintains myelin sheath

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Histidine

Front 15

Essential amino acid needed for hemoglobin formation

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Isoleucine

Front 16

Second most common amino acid found in protein

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Leucine

Front 17

Essential amino acid that lowers triglyceride levels

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Lysine

Front 18

Help initiate translation of mRNA

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Methionine

Front 19

Most abundant amino acid in the body

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Glutamine

Front 20

Transports ammonia to the liver

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Glutamine

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Product of the vreakdown of RNA

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Alanine

Front 22

Precursor for seratonin and melatonin

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Tryptophan

Front 23

Responsible for umami taste

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Glutamic acid

Front 24

Plasm aproteins are synthesized in

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Liver

Front 25

Immunoglobulins are synthesized in

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Plasma cells

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Regularly reeating structures stabilized by hydrogen bonds

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Secondary

Front 27

Enzymes to digest dietary protein

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HCL, Pepsin and trypsin

Front 28

Enzymes Dipeptidases and aminopeptidase are used to breakdown

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Oligopeptides

Front 29

Breakdown polypeptides

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Trypsin

Chymotrypsin

Elastase

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Catalyze chemical reactions

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Enzyme

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Proteins that are chemical messenger

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Hormone

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Proteins that transpory ions, molecules etc..

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Transport proteins

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Mediate the humoral immune response

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Immunoglobulin (antibodies)

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Fibrous protein are

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Structural proteins

Front 35

Proteins that serve as reserves of metal ions and amino acids that can be released and used later without harm occurring to cells

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Storage proteins

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Most widely tested storage protein

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Ferritin

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Stores iron to be later used

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Ferritin

Front 38

Plasma proteins serve as a reserve source of energy for tissues and muscle

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Energy source

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Plasma proteins function in distribution of water

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Osmotic force

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When the concentration of plasma proteins is significantly decreased, the concomitant decrease in the plasma results in____

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Increased level of interstitial fluid and edema

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Contain peptide chains composed of only amino acids

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Simple proteins

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Simple proteins may be

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Globular ir Fibrous in shape

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Simple protein shape that is soluble in water

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Globular protein

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Simple protein shape that is water insoluble

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Fibrous proteins

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Simple proteins that function as transporters, enzymes and messengers

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Globular Protein

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Consist of protein and a nonprotein

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Conjugated protein

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Nonamino part of conjugated protein

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Pristhetic group

Front 48

Conjugated protein with ion attached to the protein

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Metalloprotein

Front 49

Have cholesterol and triglyceride linked to proteins like HDL and VLDL

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Lipoproteins

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Molecules with 10% to 40% carbohydrate

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Glycoproteins

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Example of glycoproteins

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Haptoglobin, a1antitrypsin

Front 52

When percentage of carbohydrate linkedto protein is higher proteins are called

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Mucoproteins or proteoglycans

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Proteins that are combined with nuclei acid, DNA or RNA

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Nucleoproteins

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Most frequently analyzed of all proteins

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Plasma proteins

Front 55

The transport protein for thyroid hormones

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Prealbumin (transthyretin)

Front 56

Decreased in hepatic damage, acute phase inflammatory response

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Prealbumin

Front 57

A sensitive marker of poor nutritional status

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Low prealbumin level

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Prealbumin (transthyretin) is increased in patients

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Receiving steroids, alcoholism and in Chronic renal failure

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Protein present in highest concentration in plasma

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Albumin

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Measures systematic capillary efflux of albumin

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Transcapillary Escape Rate

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Responsible for nearly 80% of the colloid osmotic pressure

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Albumin

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a class of inherited errors of metabolism in which there is an enzyme defect that inhibits the body’s ability to metabolize certain amino acids

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Aminoacidopathies

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absence of activity of the enzyme phenylalanine hydroxylase (PAH), which catalyzes the conversion of phenylalanine to tyrosine

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Phenylketonuria (PKU)

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Test for PKU

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Guthrie test

Front 65

inborn metabolic disorders of tyrosine catabolism are characterized by the excretion of tyrosine and tyro- sine catabolites in urine.

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Tyrosinemia

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caused by low levels of the enzyme fumarylacetoacetate hydrolase

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Type 1 tyrosinemia

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caused by a deficiency of the enzyme tyrosine aminotransferase

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Type 2 tyrosinemia

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a rare disorder (only a few cases have been reported) caused by a deficiency of the enzyme 4-hydroxyphenylpyruvate dioxygenase

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Type 3 tyrosinemia

Front 69

test for alkaptonuria.

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Urinalysis

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____ is an inborn metabolic disease transmitted as an autosomal recessive gene, the HGD gene, which causes the lack of the enzyme homogentisate oxidase, which is needed in the metabolism of tyrosine and phenylalanine

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Alkaptonuria

Front 71

inborn metabolic disease characterized by black urine

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Alkaptonuria

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Treatment for alkaptonuria

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High dose of Vt. c

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results from an absence or greatly reduced activity of the enzyme branched-chain - -ketoacid decarboxylase, blocking the normal metabolism of the three essential branched-chain amino acids leucine, isoleucine, and valine.

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Maple syrup urine disease

Front 74

autosomal recessive metabolic disorder from a deficiency of the enzyme isovaleryl-CoA dehydrogenase, preventing normal metabolism of the branched-chain amino acid leucine.

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Isovaleric acidemia

Front 75

distinctive odor of sweaty feet

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Isovaleric acidemia