NEET MDS Lessons
Biochemistry
Positively Charged (Basic)
| Amino Acid | Side Chain Group |
|---|---|
| Lysine (K) | ε-amino group |
| Arginine (R) | Guanidino group |
| Histidine (H) | Imidazole ring (partially charged at pH 7.4) |
Mnemonic: "His Lies Are Basic" (Histidine, Lysine, Arginine)
Negatively Charged (Acidic)
| Amino Acid | Side Chain Group |
|---|---|
| Aspartate (D) | Carboxyl group |
| Glutamate (E) | Carboxyl group |
Mnemonic: "Acidic Dragons Eat" (D = Aspartate, E = Glutamate)
CLASSIFICATION OF ENZYMES
1. Oxidoreductases : Act on many chemical groupings to add or remove hydrogen atoms. e.g. Lactate dehydrogenase
2. Transferases Transfer functional groups between donor and acceptor molecules. Kinases are specialized transferases that regulate metabolism by transferring phosphate from ATP to other molecules. e.g. Aminotransferase.
3. Hydrolases Add water across a bond, hydrolyzing it. E.g. Acetyl choline esterase
4. Lyases Add water, ammonia or carbon dioxide across double bonds, or remove these elements to produce double bonds. e.g. Aldolase.
5. Isomerases Carry out many kinds of isomerization: L to D isomerizations, mutase reactions (shifts of chemical groups) and others. e.g. Triose phosphate isomerase
6. Ligases Catalyze reactions in which two chemical groups are joined (or ligated) with the use of energy from ATP. e.g. Acetyl CoA carboxylase
CALCIUM
Total calcium in the human body is 1 to 1.5kg, out of which 99% is seen in bone and 1% in extracellular fluid. The main source of calcium is milk.
The daily requirement of calcium for child is 1200mg/day and for adult it is 500mg/day. During pregnancy /lactation the calcium requirement is 1500mg/day.
The absorption of calcium takes place in 1st and 2nd part of deuodenum. Calcium absorption requires carrier protein, helped by Ca2+ - dependent ATpase.
Factors responsible for increase in calcium absorption include Vitamin D, Parathyroid hormone, acidity and amino acids. Factors such as phytic acid,oxalates, malabsorption syndromes and Phosphates decreases calcium absorption. The normal calcium level in blood is 9-11mg/dl.
Glycogenolysis
Breakdown of glycogen to glucose is called glycogenolysis. The Breakdown of glycogen takes place in liver and muscle. In Liver , the end product of glycodgen breakdown is glucose where as in muscles the end product is Lactic acid Under the combined action of Phosphorylase (breaks only –α-(1,4) linkage )and Debranching enzymes (breaks only α-(1,6) linkage )glycogen is broken down to glucose.
ZINC
The enzyme RNA polymerase, which is required for transcription, contains zinc and it is essential for protein bio synthesis.
Deficiency in Zinc leads to poor wound healing, lesions of skin impaired spermatogenesis, hyperkeratosis, dermatitis and alopecia
Ketogenic Only
| Amino Acid |
|---|
| Leucine (L) |
| Lysine (K) |
Mnemonic: "LL is Keto" (Leucine, Lysine)
Glucogenic Only
| Amino Acids |
|---|
| Most others except those listed below as ketogenic or both |
Both Ketogenic & Glucogenic
| Amino Acid |
|---|
| Isoleucine (I) |
| Phenylalanine (F) |
| Threonine (T) |
| Tryptophan (W) |
| Tyrosine (Y) |
Mnemonic: "I Prefer To Try Tasty Yogurt" (I, Phe, T, Trp, Tyr)
The Effects of Enzyme Inhibitors
Enzymes can be inhibited
- competitively, when the substrate and inhibitor compete for binding to the same active site or
- noncompetitively, when the inhibitor binds somewhere else on the enzyme molecule reducing its efficiency.
The distinction can be determined by plotting enzyme activity with and without the inhibitor present.
Competitive Inhibition
In the presence of a competitive inhibitor, it takes a higher substrate concentration to achieve the same velocities that were reached in its absence. So while Vmax can still be reached if sufficient substrate is available, one-half Vmax requires a higher [S] than before and thus Km is larger.
Noncompetitive Inhibition
With noncompetitive inhibition, enzyme molecules that have been bound by the inhibitor are taken out
- enzyme rate (velocity) is reduced for all values of [S], including
- Vmax and one-half Vmax but
- Km remains unchanged because the active site of those enzyme molecules that have not been inhibited is unchanged.