Yulia Suciati
ENVIRONMENT
ORGANISM
Ingested protein
1
Biosynthesis 2 3
Protein
a AMINO ACIDS c
Degradation (required) Nitrogen (ketogenic) Carbon skeletons (glucogenic) Used for energy pyruvate -ketoglutarate succinyl-CoA fumarate oxaloacetate
b c
Purines Pyrimidines Porphyrins
Urea
acetoacetate acetyl CoA
Amino Acid Requirements of Humans -------------------------------------------------------------------Nutritionally Essential Nutritionally Nonessential -------------------------------------------------------------------Argininea Alanine Histidine Asparagine Isoleucine Aspartate Leucine Cysteine Lysine Glutamate Methionine Glutamine Phenylalanine Glycine Threonine Proline Tryptophan Serine Valine Tyrosine --------------------------------------------------------------------a Nutritionally semiessential. Synthesized at rates inadequate to support growth of children.
NITROGEN BALANCE
Nitrogen balance = nitrogen ingested - nitrogen excreted
2. Decreased Intake
3. Lack of an essential AA
C O
COO-
NH2
R CH
C NH2
COO-
COOR
CH
COO-
oxidative decarboxylation
NH3+ R
CH2
CO2
Transamination reaction
The first step in the catabolism of most amino acids is removal of a-amino groups by enzymes transaminases or aminotransferases All aminotransferases have the same prostethic group and the same reaction mechanism. The prostethic group is pyridoxal phosphate (PPL), the coenzyme form of pyridoxine (vitamin B6)
TRANSAMINATION
ALT
Glucose-alanine cycle
Alanine plays a special role in transporting amino groups to liver.
Ala is the carrier of ammonia and of the carbon skeleton of pyruvate from muscle to liver. The ammonia is excreted and the pyruvate is used to produce glucose, which is returned to the muscle.
UREA CYCLE
mitochondria cytosol
dehydrogenase.
Enzyme is present in mitochondrial matrix. It is the only enzyme that can use either NAD+ or NADP+ as the acceptor of reducing
equivalents.
Combine action of an aminotransferase and glutamate dehydrogenase referred to as
transdeamination.
Phenylalanine hydroxylase is a mixed-function oxygenase: one atom of oxygen is incorporated into water and the other into the hydroxyl of tyrosine. The reductant is the tetrahydrofolate-related cofactor tetrahydrobiopterin, which is maintained in the reduced state by the NADH-dependent enzyme dihydropteridine reductase
Phenylketonuria
Hyperphenylalaninemia - complete deficiency of phenylalanine hydroxylase (plasma level of Phe raises from normal 0.5 to 2 mg/dL to more than 20 mg/dL). The mental retardation is caused by the accumulation of phenylalanine, which becomes a major donor of amino groups in aminotransferase activity and depletes neural tissue of -ketoglutarate. Absence of -ketoglutarate in the brain shuts down the TCA cycle and the associated production of aerobic energy, which is essential to normal brain development. Newborns are routinelly tested for blood concentration of Phe. The diet with low-phenylalanine diet.
GABA as neurotransmitter
Histidine decarboxylase
H N
Histidine
CO2
Histamine
Histamine: Synthesized in and released by mast cells Mediator of allergic response: vasodilation, bronchoconstriction
NH2 CH2 CHCOOH N H 5-OH Tryptohpan PLP CO2 HO CH2 CH2 NH2
H4 bioterin
decarboxylase
NADP+ NADPH(H+)
* Neurotransmitter * Founds in mast cells& platelets. * Vasoconstrictor for B.V.& bronchioles * Transmitter in GIT to release the peptide hormones.
HO
N H 5-OH Tryptamine (Serotonin) CH3COSCOA N-Acetyl Transferase COASH CH2CH2 NHCOCH3 N H N-acetyl 5-OH tryptamine O-methyl Transferase CH3O SAM SAH CH2CH2 NHCOCH3
N H Melatonin (N-acetyl-5-methoxy-serotonin)
Glycine produced from serine or from the diet can also be oxidized by glycine decarboxylase (also referred to as the glycine cleavage complex, GCC) to yield a second equivalent of N5,N10-methylene-tetrahydrofolate as well as ammonia and CO2.
Copy from: http://themedicalbiochemistrypage.org/amino-acid-metabolism.html
Phenylalanine
Tyrosine
Tryptophane
fumarate
Aceto acetate
Melanine
Melatonin
glucose
ketone
Thyroxin
Anthranilic
Serotonin
Alanine
Nicotinamide
Acetoacetyl CoA