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105 Cards in this Set

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  • Back

Sources of Thiamin

Pork, Legumes, Whole fortified enriched grains, sunflower seeds

Can Thiamin be effected/destroyed by any factors

Destroyed by heat and alkaline pH

What form is Thiamin found in animals foods?

Thiamin Diphosphate aka Thiamin pyrophosphate

Where is FREE Thiamin absorbed?

absorbed in the jejunum and ileum

How is the Thiamin Diphosphate converted to its free form

intestinal phosphatase removes the phosphates




Thiamin pyrophsophokinase

What are the factors that destroy Thiamin?

Thiaminases (raw fish)


Polyhydroxyphenols (tea, coffee, blueberries, brussell sprouts)




These destroy the Thiamin ring, prevented in the presence of Vitamin C and citric acid




Alcohol also inhibits absorption

Absorbed Thiamin is taken up where...

in the liver phosphorylated to TDP

What is the percentages of TDP VS TTP in the body?

80% TDP


10% as TTP

Is Thiamin carrier mediated?

Yes

What is the enzyme that converts Thiamin to it's coenzyme form TDP

thiamin pyrophosphokinase

What is the antithiamin factor that comes from raw fish? How can it be destroyed?

Thiaminases


By heat

What is the antithiamin factor that comes from coffee, tea, blueberries, brussel sprouts? How can it be destroyed?

Polyhydroxyphenols they are stable in heat but can be inhibited by Vitamin C and citric acid

Does alcohol effect Thiamin?

Inhibited by alcohol

What complexes is Thiamin's coenzyme TPP involved in?

"Dehydrogenases"




1. Pyruvate dehydrogenase comlex


2. alpha ketoglutarate dehydrogenase complex


3. BCA dehydrogenase complex

What does inhibition of Thiamin or it's coenzymes?

prevents synthesis of ATP and acetyl CoA needed for synthesis of fatty acids, cholesterol,




and allows for accumulation of lactate, pyruvate, and alpha keto gluturate

Pyruvate dehydrogenase complex overall reaction

Pyruvate + NAD+ + Coa-->


Acetyl Coa +NADH + H+ + Co2

Pyruvate Dehydrogenase complex, is _________ dependent. How?

TPP dependent


C2 of the Thiazole ring forms a carbonion making it open to a neuleophilic attack from




pyruvate


alpha keto glutarate


and other alpha ketoacids

What is the function of the Pentose Phosphate Pathway?

Synthesis of Pentose sugars and NADPH

Transketolase needs the enzyme...

TPP for the Phosphate Pentose Pathway

What is Thiamin (TPP) non coenzyme role?

Nerve conduction

RDA for Thiamin is based on...

1. Urinary excretion


2. RBC transketolase activity


3. Thiamin intake data

What is the difference between Dry and Wet Beriberi

Dry is nerve


Wet is the heart

What is the disease associated with the deficiency of Thiamin?

BeriBeri

What is the structure of Riboflavin?

flavin molecule (isoalloxazine ring) with ribotol side chain

What are the two coenzymes of Riboflavin?

FMN AND FAD

What are the food sources of Riboflavin?

Milk and milk products, eggs, meat, legumes, liver

Is Riboflavin effected by light/heat/acid/alkaline?

Destroyed by sunlight


Resistant to heat, oxidation, and acid

Riboflavin must be in _______ form for absorption

Free form only

Where is Riboflavin absorbed?

Small intestine

Is Riboflavin carrier mediated?


*** In large amounts?

Yes saturable energy dependent


In large amounts passive absorption

Does alcohol effect Riboflavin?

Alcohol inhibits

What substance stimulates absorption of Riboflavin?

Bile

In the liver Riboflavin.....

is converted to FMN and FAD after absorption

What enzymes convert Riboflavin in the liver?

Flavokinase and FAD synthetase

Free riboflavin is absorbed into..... by....

Tissues by riboflavin binding proteins

Where are the greatest sources of free Riboflavin that have been absorbed into the tissues found?

Liver, kidney, and heart

Within the cells of tissue Riboflavin is....

converted to FMN and FAD

When bound to it's apoenzyme Riboflavin is....

a Flavoprotein

What is the function of Riboflavin's coenzyme?

FMN and FAD




Oxidation/reduction reactions

Specifically how does FMN and FAD participate in oxidation/reduction reactions?

The Isoalloxazine ring accepts/donates a pair of H one electron at a time--> FMNH2 and FADH2



What are the functions of flavoproteins?

1. Electron Transport Chain


2. Vit. B6 metabolism


3. Oxidative decarboxylation of pyruvate and alpha keto glutarate


4. B oxidation, acyl Coa Dehydrogenase


5. Synthesis of THF, cofactor form of folate

The RDA of Riboflavin is based on

1. Urinary excretion


2. Relation of diet to clinical symptoms of deficiency


3. RBC glutathione reductase

What is the disease of deficiency of Riboflavin?

Ariboflavinosis (no clear characterization)


Maybe be seen in excessive alcohol

How do you test the nutriture of Riboflavin?

Measure activity of erythrocyte FAD- dependent glutathione reductase with and without FAD addition




AC greater than 1.4 = deficiency

What is the enzyme that used to assess both the RDA and the state of nutriture for riboflavin?

Erythrocyte glutathione reductase


(FAD dependent)

What is the name given tothe protein or enzymes that bind FMN and FAD?

flavoprotein?

What are the two forms of Niacin

Nicotinic Acid


and Nicotinamide

What are the food sources of Niacin?

Fish and meats


Enriched cereals and grains


Legumes and seeds

is Niacin effected by heat/acid/alkaline/light?

Minimal loss with cooking and storage

How is Niacin found in food primarily?

Nicotinamide,


nicotinic acid,


NAD+,


NADP+

What is the relationship between corn and Niacin?

only 10% of niacin available in corn because of small peptides called niacinogens

Other than food Niacin can also be found..

Synthesized in the liver from tryptophan

What % of tryptophan is metabolized to niacin?

3%

Where are free nicotinamide and nicotinic acid absorbed?

small intestine

Do nicotinamide and nicotinic acid need a carrier?

Yes, saturable carrier

In oxidation which dominates, NAD+ or NADH?

NAD+

In reduction which dominates, NADP+ or NADPH?

NADPH

What is the coenzyme role of Niacin?

Dehydrogenases require NAD and NADP as coenzymes; tightly bound to apoenzyme.




They are H+ donors and acceptors



NADH role

formed from NAD, transfers its electrons picked up from metabolic intermediates to the ETC--> ATP

NADPH role

reducing agent in biosynthesis reactions (fatty acids, cholesterol, steroid hormones)



NAD role... required for catabolism of....

Vitamin B6

Non redox role of Niacin...

DNA function and calcium signaling

The RDA for Niacin is based on..

Human depletion and repletion studies


Studies with primary urinary metabolites

What is the deficiency disease of Niacin?

Pellegra, 4 D's

Deficiency of Niacin from medications..

Isonaizid (tuberculosis) inhibits niacin synthesis




Mercaptopurine (cancer)- inhibit NAD phosphorylase

Does alcohol inhibit Niacin

no

Does Niacin have toxicity symptoms?

Yes, large doses to treat hypercholesterolemia; niacin appears to block VLDL production (not a bad thing)




Pharmacological doses--> decreased cholesterol, triglycerides and LDL, increased HDL





What is the UL of Niacin?

35 mg

How do you assess the nutriture of Niacin?

Measurement of urinary metabolite levels


RBC NAD and NADP concentrations


Plasma 2-pyridine drops with low niacin intake; indicator

What is the structure of pantothentic acid?

B-alanine and pantoic acid joined by a peptide bond




part of coenzyme A

What are the sources of pantothenic acid?

Almost all plant and animal foods


Liver kidneys, yeast, egg yolk, broccli

Is pantothenic acid destroyed be heat/light/acid/alkaline?

Easily destroyed by heating and freezing


Destroyed by acidic and alkaline solutions

Pantothenic acid is 85% of the time found as _______ in food

Coenzyme A

Where is Pantothenic Acid digested?

GI tract where it is converted to free pantothenic acid

Where is pantothenic acid absorbed?

Jejunum

Does pantothenic acid require a carrier?


High concentration vs low concentration

Passive at high


Carrier dependent at low (Sodium Dependent Multivitamin Transporter)

SMVT is shared with .... high doses of pantothenic acid....

SMVT is shared with biotin and lipoic acid.




High doses of pantothenic acid interfere with biotin absorption in the intestine and the tissue levels.

How is Pantothenic Acid transported?

Red blood cells

Where is pantothenic acid converted to Coenzyme A?

inside of the cells

Pantothenic acid functions as a component of....

1. Coenzyme A


2. 4'-phosphopantatheine





What is the structure of Coenzyme A?

Phosphoantatheine and


adenosine-3',5'-biphosphate

Coenzyme A forms _____ linkage with _______ of molecules; which ____________

Coenzyme A forms a thioester linkage with carboxylic acid of molecules which activates them

Coenzyme A can transfer the acyl groups (2-13 carbons) of....

Acetic acid


Propionic acid


methylmalonic acid


succinic acid

Coenzyme A is part of the __________ complex

Pyruvate dehydrogenase




Introduces acetate for oxidation




Joins thiamin, riboflavin, and niacin in decarboxylation of pyruvate,


alpha ketogluturate (TCA) and


succinate (TCA)

Coneyzme A transfers aceytl groups, which involves it in synthesis of...

1. Cholesterol (Acetyl CoA+ Acetoacetyl Coa)


2. Fatty acids (Acetyl CoA + CO2)


3. Bile Salts


4. Ketone bodies


5. Steroid hormones

Conenzyme A in acetylation of Nutrients: Sugars and Proteins

A. Post transitional modifications of proteins


B. Choline --> acteylcholine


C. Acetylated sugars= cell surface molecules

Coenzyme A in fatty acid synthesis via Acyl Carrier Protein (ACP)

ACP is part of Fatty Acid Synthase Complex




SH group in 4'-phosphopantatheine of ACP bind and transfer acyl group (growing fatty acid)

RDA for Pantothenic Acid

None establish

Deficiency of Pantothenic Acid

Rare

Assessment of nutriture

Urinary pantothenic acid levels reflect dietary intake as excreted intact

Raw egg whites block which vitamin?

Biotin




Because of the substance avidin which tightly binds biotin inhibiting absorption

What is the structure of Biotin?

Ureido ring and thiophene ring with valeric acid side chain

Biotin sources

Colonic bacteria


Widespread in foods


Beef, soybean, liver, (cooked) egg yolk, cereal, and legumes




In food biotin covalently bound to protein or biotin linked to lysine (biocytin)

What is biocytin

Biotin linked to lysine

Protein bound biotin is digested by... to....

Digested by Proteases into biotin and biocytin

Biocytin is digested by...

Biotinidase in intestine and plasma

Free biotin is absorbed...

proximal small intesting (jejunum mostly)

Free biotin needs a carrier?

Yes, SMVT

Sharing a transporter, panothenic acid and biotin creates a problem b/c

they have to compete and could inhibit eachother

Biotin's coenzyme role

Metabolism of Carb, amino acids, and fatty acids


-bound to 4 carboxylases

Attachment of biotin to a carboxylase requires...

Holocarboxlase synthetase

What are the four carboxylases Biotin attaches to

1. Pyruvate carboxylase


2. Propionyl CoA Carboxylase (catabolism of odd carbon fatty acids)


3. Acetyl CoA Carboxylase


4. B-methylcortonyl CoA carboxylase

Deficient in biotin-->

urinary excretion of 3-hydroxyisovaleric acid, 3-HIA

Biotin non coenzyme role

Biotinylation of hisones--> unpacking of DNA


translation of some RNAs

Assessment of Nutriture

urinary biotin excretion


increased urinary 3-HIA excretion=deficiency