Biochemistry mnemonics part one
1. AcetylCoA and acetoacetylCoA: Amino Acids Forming Them
AcetylCoA is central to many metabolic pathways and is a metabolite derived from glucose, fatty acid, and amino acid catabolism.
Acetoacetyl CoA is the precursor of HMG-CoA in the mevalonate pathway, which is essential for cholesterol biosynthesis
These CoAs are formed by a combination of amino acids which are:
"A Lighter Lease" (A LyTr LeIs):
- A=AcetylCoA or Acetoacetyl CoA
2. Adrenaline mechanism
Adrenaline is one of the fight and flight hormones, the second being noradrenaline. It is produced in adrenal medulla of the adrenal glands. It is responsible for many functions in the body examples of such are increase blood pressure, heart rate and many more.
"ABC of Adrenaline":
- Adrenaline--> activates Beta receptors--> increases Cyclic AMP
NB: it also activates alpha receptor
3. B vitamin names
Vitamin is one of the classes of food. Though required in little quantity, its deficiency or overabundance can disrupt normal body metabolism. They can be broadly divided into two which the fat soluble and water soluble vitamins.
Vitamin B is a water soluble vitamin and there are multiple of it and have different names, these are:
"The Rhythm Nearly Proved Contagious":
In increasing order:
- Thiamine (B1)
- Riboflavin (B2)
- Niacin (B3)
- Pyridoxine (B6)
- Cobalamin (B12)
NB: There are others B vitamins like B5(pantothenic acid), B7(biotin), B9(Folic acid), etc
4. BUN: Creatinine Elevation Causes
Blood urea nitrogen test measure the amount of urea nitrogen present in the blood and it indicate how properly the kidneys are functioning. Urea is a metabolic product of protein produced by the liver.
Creatinine is produced from the breakdown of muscle cell, it can also be quantified to show kidney function.
Causes of elevation are:
- Azotremia (pre-renal)
- Bleeding (GI)
- Catabolic status
- Diet (high protein parenteral nutrition)
5. Carbon monoxide: Electron Transport Chain Target
Carbon monoxide colorless, odorless, tasteless gas produced by burning gasoline, wood, propane, charcoal or other fuel. Improperly ventilated appliances and engines, particularly in a tightly sealed or enclosed space, may allow carbon monoxide to accumulate to dangerous levels.
This gas very harmful to human being when breathed because it displaces oxygen in the blood and deprives the heart, brain and other vital organs of oxygen.
• "CO blocks CO":
• Carbon monoxide (CO) blocks Cytochrome Oxidase (CO)
NB: it also blocks hemoglobin
6. Catabolism steps of branched chain amino acids
Amino acid is an organic molecule that is made up of a basic amino group (−NH2), an acidic carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each amino acid. It may be straight or branch chain. It is the building block of protein.
Steps involved in catabolism of branched chain amino acids are:
"Truck hit the Ox to Death":
- Oxidative decarboxylation
7. Citric acid cycle compounds
Citric acid cycle is a series of chemical reactions used by aerobic organisms to generate energy through the oxidation of acetate(derived from carbohydrates, fats, and proteins) into carbon dioxide.
"Oh Citric Acid Is Of (course) A SiLly STupid Funny Molecule":
"Oh! Can I Keep Some Succinate For Myself?":
- Succinyl coA
"Our City Is Kept Safe And Sound From Malice":
8. Coagulation common pathway: Factors In Order
Coagulation is an important process that ensures too much blood is not lost when there is an injury or breech in epithelial surfaces. This process take place via three pathways which are extrinsic, intrinsic and common
It should be noted that there are 13 factors responsible for coagulation. The factors responsible for common pathway are:
10 + 5 - 2 = 13
- Coagulation common pathway:
- Factor X to Factor V to Factor II to Factor XIII
9. Collagen concisely covered
Collagen is the main structural protein in the extracellular matrix(ECM) found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in body, making up from 25% to 35% of the whole-body
- C-terminal propeptide (procollagen)/ Covalent Cross links/ C vitamin/ Connective tissue/ Cartilage/ Chondroblasts/ Copper Cofactor (CovalentCross linking)
- Outside the cell is where collagen normally functions/ Osteoblasts/ Osteogenesis imperfecta
- Lysyl hydroxylase/ Lysyl oxidase (oxidatively deaminates lysyl and hydroxylysyl residues to form collagen cross links, last biosynthesis step)
- Long triple helical fibers/ Ligaments
- Alpha chains/ Attached by H bonds form triple helix/ Ascorbate for hydroxylation of lysyl and prolyl residues of pro-Alpha chains (postranslational modification)
- Gly in every third position/ Glycosylation of hydroxyl group of hydroxylysine with Glucose and Galactose; Golgi allows procollagen to Go outside of cell
- Extracellular matrix/ Eye (cornea, sclera)/ Ehlers-Danlos Syndrome
- N-terminal propeptide (procollagen)/ Nonhelical terminal extensions
Note: Procollagen LEAVEs the cell to be cLEAVEd by procollagen peptidases
10. Creatine phosphate: Amino Acid Precursors
Creatine phosphate is a muscle energy store, and spontaneously converts to creatinine which is excreted in the urine in direct proportion to muscle mass: clinically useful, such as in muscle diseases.
Amino acids precursor include:
11. Dicarboxylic acids (alpha, omega) C2 through C10: Common Names
A dicarboxylic acid is an organic compound that contain two carboxyl functional groups. The general molecular formula for dicarboxylic acids can be written as HO₂C−R2−CO₂H, where R can be aliphatic or aromatic.
"Oh My, Such Good Apple Pie, Sweet As Sugar!":
12. DNA bond strength (nucleotides)
DNA is the chemical name for the molecule that carries genetic instructions in all living things. It consists of two strands that wind around one another to form a shape known as a double helix. Each strand has a backbone made of alternating sugar (deoxyribose) and phosphate groups. Attached to each sugar is one of four bases--adenine (A), cytosine (C), guanine (G), and thymine (T). The two strands are held together by bonds between the bases; adenine bonds with thymine, and cytosine bonds with guanine.
- Strongest bonds are between Cytosine and Guanine, strong like Crazy Glue (3 H-bonds), whereas the A=T only have 2 H-bonds.
This is relevant to DNA replication, as the weaker A=T will be the site where RNA primer makes the initial break.
13. Electron transport chain: Rotenone's Site Of Action
Electron transport chain is a series of electron transporters located in the inner mitochondrial membrane that transports electrons from NADH and FADH2 to molecular oxygen. In the process, protons are pumped from the mitochondrial matrix to the intermembrane space, and oxygen is reduced to form water.
The three major steps include:
- Step 1: Generating a Proton Motive Force.
- Step Two: ATP Synthesis via Chemiosmosis.
- Step Three: Reduction of Oxygen.
- Summary: Oxidative Phosphorylation.
The site of action:
- Rotenone is a site specific inhibitor of complex one
14. Enzyme kinetics: Competitive Vs. Non-Competitive Inhibition
Enzyme kinetics is the study of enzyme reactions rates and the conditions which affect them. Michaelis-Menten kinetics is a model of enzyme kinetics which explains how the rate of an enzyme-catalysed reaction depends on the concentration of the enzyme and its substrate.
Enzymes may competitively or non-competitively inhibit its substrate, therefore,
- With Kompetitive inhibition: Km increases; no change in Vmax.
- With Non-kompetitive inhibition: No change in Km; Vmax decreases.
15. Enzymes: Classification
Enzymes are biological catalysts which increase the rate of chemical reaction without being used up themselves. They are a vital component of the cell because without them, many biological reactions would be too slow to sustain life.
Classification of enzymes are:
"Over The HILL":
16. Enzymes: Competitive Inhibitors
Check the above for brief description of enzymes:
- "Competition is hard because we have to travel more kilometers (Km) with the same velocity":
- With competitive inhibitors, velocity remains same but Km increases
17. Essential amino acids
Check number 6 for description of amino acids. However, amino acids can be divided into essential, semi-essential and non-essential.
The following are essential amino acids
PVT. TIM HALL:
Arg and His are considered semi-essential.
18. Fabry's disease
Fabry’s disease is also known as Anderson–Fabry disease, is a rare lysosomal storage diseases.that can affect many parts of the body, including the kidneys, heart, and skin.
- Foam cells found in glomeruli and tubules/ Febrile episodes
- Alpha galactosidase A deficiency/ Angiokeratomas
- Burning pain in extremities/ BUN increased in serum/ Boys
- Renal failure
- YX genotype (male, X linked recessive)
19. Fasting state: Branched-Chain Amino Acids Used By Skeletal Muscles
Fasting state also known as post-absorptive state occurs when the food has been digested, absorbed, and stored. One commonly fast overnight, but skipping meals during the day puts your body in the post-absorptive state as well. During this state, the body must rely initially on stored glycogen.
Amino acids are also used during this period, the once used by skeletal muscles are:
"Muscles LIVe fast":
20. Folate deficiency: Causes
Folate or vitamin B9 is a form of a water- soluble vitamin. Folate occurs naturally in food, and folic acid is the synthetic form of this vitamin. Its deficiency can result in anaemia.
A FOLIC DROP:
- Folic acid antagonists
- Oral contraceptives
- Low dietary intake
- Infection with Giardia
- Celiac sprue
- Relative folate deficiency
21. Galactosaemia: Enzyme Deficiency
Galactosemia, which means “galactose in the blood,” is a group of inherited disorders that impair the body's ability to process and produce energy from galactose. This is as a result of an enzyme deficiency.
The enzyme is:
- Galactose 1 Phosphate Uridyl Transferase.
NB: There is an assay called the Galiput test for this.
22. Glucagon function
Glucagon is a peptide hormone, produced by alpha cells of the pancreas which raises concentration of glucose and fatty acids in the bloodstream, and is considered to be the main catabolic hormone of the body.
- "Mr. Gluca has Gone to the cAMP to bring out some Glucose":
- Glucagon elevates glucose by cAMP mechanism.
23. Glycogen storage: Anderson's (IV) Vs. Cori's (III) Enzyme Defect
Glycogen storage disease ( GSD) is a genetic condition in which the body deficient of various enzymes that metabolize glycogen resulting in its build up in the body. There are eight types of GSD.
The difference between type IV and III are:
- Anderson's=Branching enzyme.
- Cori's=Debranching enzyme.
Otherwise, can't really distinguish clinically.
24. Glycogen storage: Names Of Types I Through VI
Check 24 for brief description of glycogen storage diseases.
"Viagra Pills Cause A Major Hardon":
- Von Gierke's
25. Glycolysis steps
Glycolysis is a cytoplasmic pathway which breaks down glucose into two three-carbon compounds and generates energy.
"Goodness Gracious, Father Franklin Did Go By Picking Pumpkins (to) Prepare Pies":
- 2-Phosphoglycerate (to)
- Phosphoenolpyruvate [PEP]