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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)

Vitamin B12: Cobalamin

Vitamin B12, also known as cobalamin, aids in the building of genetic material, production of normal red blood cells, and maintenance of the nervous system.

RDA The Recommended Dietary Allowance (RDA) for vitamin B12 is 2.4 mcg/day for adult males and females

Vitamin B12 Deficiency

Vitamin B12 deficiency most commonly affects strict vegetarians (those who eat no animal products), infants of vegan mothers, and the elderly. Symptoms of deficiency include anemia, fatigue, neurological disorders, and degeneration of nerves resulting in numbness and tingling.

Enzyme Kinetics

Enzymes are protein catalysts that, like all catalysts, speed up the rate of a chemical reaction without being used up in the process. They achieve their effect by temporarily binding to the substrate and, in doing so, lowering the activation energy needed to convert it to a product.

The rate at which an enzyme works is influenced by several factors, e.g.,

  • the concentration of substrate molecules (the more of them available, the quicker the enzyme molecules collide and bind with them). The concentration of substrate is designated [S] and is expressed in unit of molarity.
  • the temperature. As the temperature rises, molecular motion - and hence collisions between enzyme and substrate - speed up. But as enzymes are proteins, there is an upper limit beyond which the enzyme becomes denatured and ineffective.
  • the presence of inhibitors.
    • competitive inhibitors are molecules that bind to the same site as the substrate - preventing the substrate from binding as they do so - but are not changed by the enzyme.
    • noncompetitive inhibitors are molecules that bind to some other site on the enzyme reducing its catalytic power.
  • pH. The conformation of a protein is influenced by pH and as enzyme activity is crucially dependent on its conformation, its activity is likewise affected.

The study of the rate at which an enzyme works is called enzyme kinetics.

ISO-ENZYMES

Iso-enzymes are physically distinct forms of the same enzyme activity. Higher organisms have several physically distinct versions of a given enzyme, each of which catalyzes the same reaction. Isozymes arise through gene duplication and exhibit differences in properties such as sensitivity to particular regulatory factors or substrate affinity that adapts them to specific tissues or circumstances.

Isoforms of Lactate dehydrogenase is useful in diagnosis of myocardial infarction. While study of alkaline phosphatase isoforms are helpful in diagnosis of various bone disorder and obstructive liver diseases.

Glutathione

  • Structure: A tripeptide made of Glutamate, Cysteine, and Glycine (linked as Glutamyl-Cysteinyl-Glycine).

  • Function:

    • Major antioxidant in cells—neutralizes reactive oxygen species (ROS).

    • Involved in detoxification, immune function, and redox signaling.

  • Fun Fact: Exists in reduced (GSH) and oxidized (GSSG) forms—its ratio is a marker of oxidative stress.

 Creatinine

  • Synthesis: Derived from Glycine, Arginine, and Methionine via creatine metabolism.

  • Function:

    • Waste product of muscle metabolism.

    • Excreted by kidneys—used as a marker of renal function in blood tests.

  • Clinical Insight: Elevated serum creatinine often signals impaired kidney function.

Calcium-Binding Proteins

1. Troponin-C

  • Role: Part of the troponin complex in skeletal and cardiac muscle.

  • Function: Binds calcium to initiate muscle contraction by enabling actin-myosin interaction.

  • Clinical Use: Troponin levels are measured to diagnose myocardial infarction.

2. Calmodulin

  • Structure: Small, highly conserved protein with 4 calcium-binding sites.

  • Function:

    • Acts as a calcium sensor and regulator.

    • Modulates activity of enzymes, ion channels, and other proteins in response to calcium levels.

  • Versatility: Involved in smooth muscle contraction, metabolism, memory formation, and more.

PHOSPHORUS

Serum level of phosphate is 3-4 mg/dl for adults and 5-6 mg/dl in children. Consumption of calcitriol increases phosphate absorption.

Functions of phosphorus
(a) Plays key role in formation of tooth and bone

(b) Production of high energy phosphate compounds such as ATP, CTP, GTP etc.,

(c) Synthesis of nucleotide co-enzymes such as NAD and NADP

(d) Formation of phosphodiester backbone structure for DNA and RNA synthesis

Hypophosphatemia is the condition which leads to decrease in absorption of phosphorus. it leads to hypercalcamia

Hyperphosphatemia, increase in absorption of phosphate was noticed. Hyperphosphatemia leads to cell lysis, hypocalcemia and thyrotoxicosis.

STEROIDS
Steroids  are the compounds containing a cyclic steroid nucleus  (or ring) namely cyclopentanoperhydrophenanthrene (CPPP).It consists of a phenanthrene  nucleus (rings A, B and C) to which a cyclopentane ring (D)  is attached.

Steroids  are the compounds containing a cyclic steroid nucleus  (or ring) namely cyclopentanoperhydrophenanthrene (CPPP).It consists of a phenanthrene  nucleus (rings A, B and C) to which a cyclopentane ring (D)  is attached.

There are several steroids in the biological system. These include cholesterol, bile acids, vitamin D, sex hormones, adrenocortical hormones,sitosterols, cardiac glycosides and alkaloids

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