Six Amino Acids Are Degraded to Pyruvate

The carbon skeletons of six amino acids are converted in whole or in part to pyruvate. The pyruvate can then be converted to either acetyl-CoA (a ketone body precursor) or oxaloacetate (a precursor for gluconeogenesis). Thus amino acids catabolized to pyruvate are both ketogenic and glucogenic.

The six are Alanine Tryptophan Cysteine Serine Glycine threonine

Vitamin-Coenzymes in Amino Acid Metabolism

Vitamin B-6 (pyridoxal phosphate) Folic acid (tetrahydrofolate) Vitamin B-12

Vitamin-Coenzymes in Amino Acid Metabolism

Vitamin B-6 : pyridoxal phosphate Enzymes that bind amino acids use PLP as coenzyme for binding Transaminases Amino acid decarboxylases Amino acid deaminases

Vitamin-Coenzymes in Amino Acid Metabolism

Folacin: Tetrahydrofolate (THF)
Carrier of single carbons
Donor & receptor Glycine and serine Tryptophan degradation Histidine degradation Purine and pyrimidine synthesis

Alanine & Cysteine

Alanine yields pyruvate directly on transamination with-ketoglutarate, and the side chain of tryptophan is cleaved to yield alanine and thus pyruvate. Cysteine is converted to pyruvate in two steps; one removes the sulfur atom, the other is a transamination.

COO CH2 CH3 HC NH3+ CH2 CH3 O C O

COO CH2 CH2

HC

NH3+

COO

COO

COO

COO

alanine

pyruvate glutamate Aminotransferase (Transaminase)

a-ketoglutarate

The 3-C a-keto acid pyruvate is produced from alanine, cysteine, glycine, serine, & threonine. Alanine deamination via Transaminase directly yields pyruvate.

A metabolic flow chart illustrating the position of CDO within the many pathways of cysteine metabolism.

Glycine
Glycine is degraded via three pathways, only one of which leads to pyruvate. Glycine is converted to serine by enzymatic addition of a hydroxymethyl group. This reaction, catalyzed by serine hydroxymethyl transferase, requires the coenzymes tetrahydrofolate and pyridoxal phosphate. In the second pathway, which predominates in animals, glycine undergoes oxidative cleavage to CO2, NH4 , and a methylene group (-CH2-). This readily reversible reaction, catalyzed by glycine cleavage enzyme (also called glycine synthase), also requires tetrahydrofolate, which accepts the methylene group.

 In this oxidative cleavage pathway the two carbon atoms of glycine do not enter the citric acid cycle. One carbon is lost as CO2 and the other becomes the methylene group of N5,N10-methylenetetrahydrofolate, a one carbon group donor in certain biosynthetic pathways.

Threonine
There are two significant pathways for threonine degradation. One pathway leads to pyruvate via glycine. The conversion to glycine occurs in two steps, with threonine first converted to 2-amino-3 ketobutyrate by the action of threonine dehydrogenase. This is a relatively minor pathway in humans, accounting for 10% to 30% of threonine catabolism, but is more important in some other mammals. The major pathway in humans leads to succinyl-CoA and is described later.

 Threonine is cleaved to acetaldehyde and glycine by threonine aldolase. Acetaldehyde is then oxidized to acetate which is converted to acetyl CoA. Glycine is catabolized as described earlier.

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