Catabolism of L-tyrosine by the homoprotocatechuate pathway in gram-positive bacteria.

A metabolic pathway for L-tyrosine catabolism involves 3,4-dihydroxyphenylacetic acid (homoprotocatechuic acid) as substrate for fission of the benzene nucleus. Cell extracts of an organism tentatively identified as a Micrococcus possessed the enzymes required for degrading homoprotocatechuate to succinate and pyruvate, and stoichiometry was established for several of these reactions. When the required coenzymes were added, cell extracts degraded L-tyrosine to the ring-fission product of homoprotocatechuate 2,3-dioxygenase and also converted 4-hydroxyphenylpyruvic acid into 4-hydroxyphenylacetic acid. This compound, in turn, gave stoichiometric amounts of the ring-fission product of homoprotocatechuate by the action of a nicotinamide adenine dinucleotide phosphate-dependent 3-hydroxylase coupled with homoprotocatechuate 2,3-dioxygenase. Evidence is presented that this route for L-tyrosine catabolism is taken by five other gram-positive strains, including Micrococcus lysodeikticus and a species of Bacillus. Five other gram-positive bacteria from other genera employed the alternative homogentisate pathway.