GLYCINE - PowerPoint PPT Presentation

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GLYCINE

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BIOCHEMISTRY – PowerPoint PPT presentation

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Title: GLYCINE


1
  • GLYCINE

M.Prasad Naidu MSc Medical Biochemistry, Ph.D.Rese
arch Scholar
2
  • GLYCINE
  • It is simplest aminoacid
  • Nonessential and glucogenic.
  • Formation of glycine
  • From serine
  • From threonine
  • By glycine synthase reaction

3
  • By Glycine synthase
  • NADH H NAD
  • CO2 NH4
    glycine
  • N5 , N10 methylene THF THF
  • Glycine synthase is a multienzyme complex and
    requires PLP , NAD and THF.

4
  • Metabolic functions of glycine
  • Glycine is used for biosynthesis of
  • Heme
  • Purine ring
  • Creatine
  • 4. Glutathione
  • 5. As a conjugating agent
  • 6. Glycine as neurotransmitter
  • 7.Glycine as a constituent of protein

5
  • 1.Heme synthesis
  • ALA synthase
  • glycine succinyl CoA
    d-aminolevulinate
  • PLP
  • This is the rate limiting step in heme synthesis.

6
2. Purine ring the whole molecule of glycine is
incorporated into purine ring (C4 ,C5 and N7).

synthetase 5-phosphoribosyl-1-a
mine glycinamide
ribonucleotide GLYCINE
ATP ADP Pi
7
  • 3. Synthesis of creatine
  • Arginine Glycine
  • Kidney
    Arginine- glycine transamidinase
  • Guanidoacetate
  • Guanidoacetate methyltransferase
    Liver
  • Creatine

  • Creatine kinase
  • Creatine Phosphate

SAM
SAH
H2O
ATP
CREATININE
ADP
MUSCLE
Pi
8
  • Creatine is reversibly phosphorylated to
    creatine phosphate by creatine kinase and stored
    in muscle as high enegy phosphate.
  • Creatinine
  • it is anhydride of creatine
  • it is formed by cyclisation of creatine.

9
  • Serum creatinine 0.7 -1.4
    mg/dl
  • Urine creatinine 1- 2 g/day
  • Serum creatinine concentration is not
    influenced by endogenous or exogenous factors, so
    used as a more reliable indicator of renal
    function.

10
4.Synthesis of glutathione
11
  • Superoxide dismutase Peroxidase
  • O2- (superoxide) H2O2 H2O
  • i)Freeradical scavenging 2GSH GS
    SG
  • Glutathione reductase
  • 2NADP NADPHH
  • Glucose -6-phosphate GPD
  • By scavenging free radicals it maintains RBC
    membrane integrity.

12
  • iii)Involved in amino acid transport Meister
    cycle
  • iv)Insulin inactivation by
  • hepatic insulin glutathione transhydrogenase
  • Insulin(AB chains) 2GSH GSSGA
    chain B chain
  • v) Activation of enzymes Many enzymes having
    SH in active site are kept in the active form by
    glutathione.
  • Ex glyceraldehyde -3-P dehydrogenase

13
  • vi)Met-hemoglobin glutathione is necessary for
    the reduction of met-Hb(ferric) normal Hb
    (ferrous state). The met-Hb is can not transport
    oxygen .
  • 2Met-Hb-(Fe3 ) 2 GSH 2 Hb-(Fe2) 2H
    GSSG

14
  • 5. Conjugating agent
  • It is used for conjugating bile acids so that
    their amphipathic property is increased.
  • Cholic acid Glycine
    glycocholic acid
  • Chenodeoxycholic acid
    glycochenodeoxycholic
  • Glycine
    acid
  • Glycine Benzoic acid
    benzoyl glycine

  • ( hippuric acid)

15
  • 6.Glycine as neurotransmitter
  • It is a neurotransmitter in the brainstem and
    spinal cord.
  • At moderate levels it disrupts neuronal traffic
    but at very high levels it causes overexcitation

16
7.Glycine as a constituent of protein
  • It is seen where the polypeptide chain bends or
    turns.
  • In collagen , every third aminoacid is glycine.
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