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Carbohydrate

Major: Glucose. No essential. 4cal/gm. Stored as glycogen in muscle and liver

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Lipid

Essential: Linolenic and linoleic acid. 9 cal/gm. Stored as TG mainly in adipose

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Protein

Made of AA. 9 are essential. 4cal/gm. No storage of free FA, carbons converted to glycogen orTG, nitrogen goes to urea

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Alcohol (ethanol)

7cal/gm. Stored as TG

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Vitamins

Essential, not altered in reaction. Function: rxn cofactor

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Basal Metabolic Rate (BMR)

Energy req. to keep all organs function while at rest. 24*(weight in kg)+ energy for work (1.3, 1.6, 2)

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Body mass index

(Weight in Kg)/(hight in m)^2 or 703*(weight in lbs.)/(height in inch.)^2

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unhealthy BMI

<18.5

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normal BMI

18.6-25

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pre-obese BMI

25.1-30

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obese BMI

30.1-39.9

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morbidly obese

>40

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ATP

Major energy source. Contains 2 high energy bonds which are worth 7kcal/mole when hydrolyzed

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Creatine-P

High energy storage molecule that muscle uses. Donates P to ADP under rapid muscle contraction to make ATP

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Glycogen

Storage form of glucose in liver and muscle

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Oxidative Phosphorylation

Generates energy from transferring electrons to oxygen

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FA

Preferred energy storage form (in form of TG). Can make KB. Cannot make sugars. Long hydrocarbons (3-24) with a carboxylic acid tail (amphipathic)

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HMP shunt

Alternative means of glucose oxidation. Convert 6 and 5 carbons sugars. Generate NADPH

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Enzymes

Proteins that aid in substrate reaching transition state, reduce energy required. Do NOT change overall equilibrium constant. Pathway regulation

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Futile cycles

Also called substrate cycling. Opposing pathways are active at same time. Ex. Glycolysis and gluconeogenesis.

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Enzymes released with heart damage

CPK and troponin

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Enzymes released with pancreatic damage

Amylase

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Enzymes released with liver damage

AST and ALT

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Bis- Vs. Di-

Bis=same functional group on different atoms in same molecule. Di= same functional group on same atom or linked together then attached to one atom

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NAD+

Derived from Niacin (has reactive site), ribose and adenine

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Michaelis-Menton Eq.

v=(Vmax)/(1+[Km/[S]])

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Km

1/2 Vmax. Substrate concentration required for enzyme to reach 1/2 Vmax

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Lineweaver-Burk Deviation

Michaelis-Menton equation in straight line. Y=mx+b. 1/v = (Km/Vmax)(1/[S]) + (1/Vmax). Slope is altered by 1+ [Inhibitor]/Ki. (Ki = inhibitor dissociation constant)

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Competitive inhibitor

Competes for substrate binding site. Increases Km