Compare & Recall: High-Yield Biochemistry Tables for NEET PG

S no.

Organelle

Marker Enzyme

1

Nucleus

Replication-DNA polymerase Transcription- RNA polymerase

2

Endoplasmic Reticulum

Glucose-6-Phosphatase

3

Golgi Complex

Galactosyl transferase

4

• Mitochondria
• Outer Membrane (OM)
• Inner Membrane

For OM - Monoamine oxidase

For inner membrane - ATP synthase / Succinate dehydrogenase

5

Lysosome

Cathepsin

6

Cytoplasm

Lactate dehydrogenase

7

• Peroxisome:

ᴑ Very long chain fatty acid oxidation, concerned with ether lipid synthesis (Plasmalogen).

ᴑ Related to alpha oxidation of BCFA (defect leads to Refsum's Disease).

Catalase

S. No

NADH

NADPH

1

• Can enter into ETC and give rise to 2.5 ATPs. It is going to be a part of Oxidative Phosphorylation.

• Necessary for reductive biosynthesis of all lipids. 
• It is also necessary for regenerating Glutathione which is an important antioxidant mechanism of RBCs. 
• Necessary as a coenzyme for Ribonucleotide Reductase 
• Necessary as a coenzyme for Cytochrome P450 Enzymes 

2

Sources- all fuel Oxidative pathways. 

• Glycolysis 
• PDH
• Citric Acid Cycle 
• Amino acid oxidation 

Sources-

• The major source of it HMP Shunt
• Minor sources include Cyt ICDH 
• Malic Enzyme 

Benedict's Solution

Fehling's Solution

• Detects the presence/absence of reducing substance in a given solution

• Detects the presence/absence of reducing substance in a given solution

• Copper sulphate (blue colour)
• Sodium carbonate (Alkaline medium).
• Sodium citrate (Stabilizes the solution).

• Fehling's A- Copper sulphate
• Fehling's B- Sodium hydroxide (Stronger alkaline medium- facilitates reduction property more)
• Fehling's C- Sodium Potassium Tartrate.

• No auto-reduction

• Fehling's B is a stronger alkaline medium; it causes a reduction of CuSO4 to give red color. This process is called auto-reduction.
• Therefore, we keep 3 solutions separately to prevent auto reduction.

• Simpler and easier

• Practically difficult to prevent auto reduction

Point Mutation

Frameshift Mutation

• One nucleotide is substituted by other.
• Depending on the nucleotide substitution it is divided into
• Transition:

• Purine is replaced with a purine.
• Pyrimidine is replaced with pyrimidine
• Transversion:

• Purine is replaced with pyrimidine.
• Pyrimidine is replaced with purine

• When there is a loss or gain of nucleotides the entire frame of reading will be shifted.
• It has two types.
• Deletion:

• Loss of nucleotide
• Insertion:

• Gain of nucleotide

Step-01

Tryptophan → Formylkynurenine

• Catalyzed by tryptophan pyrrolase

Step-02

Formylkynurenine → Kynurenine

Step-03

Kynurenine → 3-OH Kynenurine

• Catalyzed by formyltransferase
• Converts tetrahydrofolate to formyl tetrahydrofolate
• It enters one carbon pool and is used to form C2 of purine rings.

Step-04

3-OH Kynenurine → 3-OH Anthranilic acid

• Catalyzed by Kynenurinase and dependent on B6 (pyridoxal phosphate)

Step-05

3-OH Anthranilic acid → Quinolinate

• 3-OH Anthranilic acid undergoes a series of non- enzyme catalase chemical reactions to form a ring (quinolinate)

Step-06

Quinolinate → Niacin Mono Nucleotide (NMN)

• Rings get attached to ribose 5-phosphate in the presence of quinolinate phosphoribosyl transferase (QPRTASE) and forms nucleotide