Glycine, Serine

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Glycine , serine,

Glycine
• Simplest AA
• Non essential
• Glucogenic
• Formed from SERINE
THREONINE
GLUTAMATE
ALANINE
• UTILISED BY
• GLYCINE CLEAVAGE SYSYTEM= COMPLETELY DEGRADED TO CO2
AMMONIA AND ONE CARBON FOLATE DERIVATIVE
• GLYCINE IS CHANNELED TO GLUCOGENIC PATHWAY BY FIRST
CONVERTING TO SERINE
Glycine cleavage system
Deamination of serine to pyruvate.
Metabolic Functions of Glycine
Glycine may be used for the biosynthesis of the following
compounds and activities
• Creatine, creatine phosphate and creatinine
• Heme
• Purine nucleotides
• Glutathione
• Inhibitory neurotransmitter
• Conversion to serine
• Conjugation of bile acids
• glycine cleavage system
• Glucogenic.
Creatine Kinase
Muscle -- MM -- Muscular dystrophy
Brain -- BB
Heart -- MB -- Myocardial infarction

Creatine phosphate is the stored energy in muscle


Creatine
Urinary Creatine excretion
Normal : Negligible
Increased in
Muscle dystrophy
Muscle injuries
Increased in muscle dystrophy
Serum Creatinine
0.7 to 1.4 mg / dl for Male
0.6 to 1.3 mg / dl for Female
Increased in Renal failure
Serum level usually parallels
the severity of the disease

Better index for renal diseases than blood urea


Clinical Applications of Creatinine and Creatine
Normal serum creatinine level is 0.7 to 1.4 mg/dL and serum
creatine level is 0.2–0.4 mg/dL.

Creatinine level in blood is a sensitive indicator of renal function. As the


kidney function is decreased, correspondingly blood creatinine level is
increased.

Urine contains negligible amount of creatine in normal males. But in the


early phase of muscular dystrophies, the blood creatine and urinary
creatinine are increased. In the end stages of muscular dystrophy, as the
muscle mass is considerably reduced, the creatinine level is lowered.
• Apart from the muscular dystrophies, reduced muscle mass is also the
cause for low creatinine in (a) women, (b) old age, (c) bedridden states
and d) low protein diet.
• The enzyme creatine kinase (CK), especially the cardiac
isoenzyme (CK-MB) is elevated in myocardial infarction.
Special Metabolic Functions
• Biosynthesis of
Heme
Creatine
Purine nucleotides
Glutathione
• Acts as a neurotransmitter
In brain stem and spinal cord

• Is a constituent of protein
In collagen, every 3rd amino acid is glycine
Disorders due to Defective Glycine Metabolism
1. Non ketotic hyperglycinemia
• Defect in glycine cleavage system
• Glycine level increased in blood, urine & CSF
• Severe mental retardation & seizures
• No effectve management
2. Primary Hyperoxaluria
Serine
• Aliphatic hydroxy amino acid
• Non essential
• Glucogenic

• Formed from glycine


• alanine
• Catabolism of Serine
1. Deamination to pyruvate
2. Transamination to hydroxypyruvate
3. Serine is glucogenic.

• Importance of serine
• Formation of choline
• Component of proteins
Choline Synthesis
• A. Serine is involved in the formation of choline
• B. Choline is used for acetylcholine synthesis, which is an important
neurotransmitter.
Selenocysteine (SeCys) (21st Amino Acid)
• Selenocysteine is abbreviated as SeCys.
• It is seen at the active site of the following enzymes:
a) Thioredoxin reductase;
b) Glutathione peroxidase, which scavenges peroxides;
c) De-iodinase that removes iodine from thyroxine to make
triiodothyronine and
d) Selenoprotein P, a glycoprotein seen in mammalian blood.
• Their concentration falls in selenium deficiency.
Alanine (ALA) (A)

• Alanine is a non-essential glucogenic amino acid.


• Alanine can be formed by transamination of pyruvate.
• The enzyme is alanine amino transferase (ALT).
• ALT level in blood is increased in liver diseases.
• Under conditions of starvation, the glucose alanine cycle is of special
metabolic significance.
• Alanine is quantitatively the most important amino acid taken up by the liver
from peripheral tissues, particularly from skeletal muscle.
• It forms a major participant in interorgan transport of nitrogen.
Threonine (THR) (T)
• It is an essential amino acid. It is glucogenic.
• Threonine does not directly undergo transamination, but undergoes
deamination forming alpha ketobutyric acid.
• The enzyme is threonine dehydratase.
• The OH group of threonine residue in protein serves to provide a site
for phosphorylation (as in the case of serine).
• This OH group also serves for combining carbohydrate residues to
proteins, so as to make glycoproteins.

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