Key Reactions In Amino Acid Biosynthesis Flashcards
Common features in amino acid biosynthesis
Transamination
One-carbon transfers
Transamination
The transfer of amino groups from one molecule to another; an important process in the anabolism and catabolism of amino acids
Citric acid cycle
Closely associated with amino acid metabolism
(a-ketoglutarate, pyruvate, acetyl-CoA)
Amphibolic (anabolic and catabolic)
Glutamate dehydrogenase and glutamine sythetase similarity and difference
Both responsible for most of NH4 assimilation
GS has lower Km than GDH
(Low nitrogen concentration - GS reaction favored)
Pyridoxal phostohate
Active form of VitB6
Catalyses transamination and decarboxylation and racemazation reactions
All reactions are reversible
PyrP mechanism
PyrP forms imine with a-amino group of amino acid
Rearrangement gives isometric imine
Hydrolysis give a-ketoacid and pyradoxamine
Pyradoxamine forms schiff base with acceptor substrate
Rearrangement and hydrolysis result in new amino acid and PyrP regenerated
Imine
Schiffs base
Racemazation reaction
Conversion of amino acids from the L-form to D-form
Creates quinonoid intermediate
Transfer of one carbon unit
One-carbon transfer
Enzyme for serine (serine hydroxymethylase)
The one-carbon acceptor is tetrahydrofolate (folic acid derivative)
Reduction of folic acid
Tetrahydrofolic acid (THF)
THF 3 parts
Pteridine ring
P-aminobenzoic acid
Glutamic acid
Serine one carbon transfer equation
Serine + tetrahydrofolate —> glycine + methylenetetrahydrofolate + H2O
Other one carbon carriers
S-adenosylmethionine (SAM)
Cobalamine (Vit B12)
Biotin (Vit B7 or Vit BH)
SAM
Results in S-adenohomocystein
Which is Hydrolysed into homocysteine
Homocysteine and serine result in cysteine
Only pathway for cysteine production in animals
Cobaline
Vit B12
Generates tetrahydrofolate and methionine
Helps produce nucleic acids and red blood cells
Deficiency results in anaemia