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J Bacteriol. Jul 1976; 127(1): 362–366.
PMCID: PMC233070

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.

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Selected References

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  • Adachi K, Iwayama Y, Tanioka H, Takeda Y. Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens. Biochim Biophys Acta. 1966 Apr 12;118(1):88–97. [PubMed]
  • Adachi T, Murooka Y, Harada T. Derepression of arylsulfatase synthesis in Aerobacter aerogenes by tyramine. J Bacteriol. 1973 Oct;116(1):19–24. [PMC free article] [PubMed]
  • CHAPMAN PJ, DAGLEY S. Oxidation of homogentistic acid by cell-free extracts of a vibrio. J Gen Microbiol. 1962 Jun;28:251–256. [PubMed]
  • DAGLEY S, GIBSON DT. THE BACTERIAL DEGRADATION OF CATECHOL. Biochem J. 1965 May;95:466–474. [PMC free article] [PubMed]
  • Devi NA, Kutty RK, Vasantharajan VN, Subba RAO PV. Microbial metabolism of phenolic amines: degradation of dl-synephrine by an unidentified arthrobacter. J Bacteriol. 1975 Jun;122(3):866–873. [PMC free article] [PubMed]
  • Hareland WA, Crawford RL, Chapman PJ, Dagley S. Metabolic function and properties of 4-hydroxyphenylacetic acid 1-hydroxylase from Pseudomonas acidovorans. J Bacteriol. 1975 Jan;121(1):272–285. [PMC free article] [PubMed]
  • Hopper DJ, Chapman PJ, Dagley S. Enzymic formation of D-malate. Biochem J. 1968 Dec;110(4):798–800. [PMC free article] [PubMed]
  • Hopper DJ, Chapman PJ, Dagley S. Metabolism of l-Malate and d-Malate by a Species of Pseudomonas. J Bacteriol. 1970 Dec;104(3):1197–1202. [PMC free article] [PubMed]
  • Hopper DJ, Chapman PJ, Dagley S. The enzymic degradation of alkyl-substituted gentisates, maleates and malates. Biochem J. 1971 Mar;122(1):29–40. [PMC free article] [PubMed]
  • Leung PT, Chapman PJ, Dagley S. Purification and properties of 4-hydroxy-2-ketopimelate aldolase from Acinetobacter. J Bacteriol. 1974 Oct;120(1):168–172. [PMC free article] [PubMed]
  • Norris DB, Trudgill PW. The metabolism of cyclohexanol by Nocardia globerula CL1. Biochem J. 1971 Feb;121(3):363–370. [PMC free article] [PubMed]
  • ROSENBERGER RF, ELSDEN SR. The yields of Streptococcus faecalis grown in continuous culture. J Gen Microbiol. 1960 Jun;22:726–739. [PubMed]
  • Sparnins VL, Chapman PJ, Dagley S. Bacterial degradation of 4-hydroxyphenylacetic acid and homoprotocatechuic acid. J Bacteriol. 1974 Oct;120(1):159–167. [PMC free article] [PubMed]
  • Sparnins VL, Dagley S. Alternative routes of aromatic catabolism in Pseudomonas acidovorans and Pseudomonas putida: gallic acid as a substrate and inhibitor of dioxygenases. J Bacteriol. 1975 Dec;124(3):1374–1381. [PMC free article] [PubMed]

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