PubMed · 6433662
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L Que. 1983. The catechol dioxygenases.. https://pubmed.ncbi.nlm.nih.gov/6433662/
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Salmonella typhimurium was shown to use the gentisate pathway to metabolize m-hydroxybenzoate and gentisate, m-Hydroxybenzoate hydroxylase and gentisate 1,2-dioxygenase were induced by growth on either gentisate or m-hydroxybenzoate. These enzymes were not detected when the bacteria were grown with glucose or glucose and either m-hydroxybenzoate or gentisate. However, both enzymes were induced when the bacteria were grown on succinate with either substrate. The maleylpyruvate isomerase required reduced glutathione and was irreversibly inhibited by N-ethylmaleimide.
One of the three components of the naphthalene dioxygenase occurring in induced cells of Pseudomonas sp. strain NCIB 9816 has been purified to homogeneity. The protein contained 2 g-atoms each of iron and acid-labile sulfur and had an apparent molecular weight of 13,600. The evidence indicates that it is a ferredoxin-type protein that functions as an intermediate electron transfer protein in naphthalene dioxygenase activity.
Two bacterial strains excreting a yellow pigment were isolated from human urine and identified as Serratia marcescens. The pigment was produced in the late exponential and early stationary phases of growth. Minimal media supplemented with tyrosine, phenylalanine, 3,4-dihydroxyphenylacetate or tryptophan, as well as complex media, induced pigment production. UV-visible spectra of the extracted pigment had peaks characteristic of 2-hydroxy-5-carboxymethylmuconate semialdehyde, produced from meta-cleavage of 3,4-dihydroxyphenylacetate by the enzyme 3,4-dihydroxyphenylacetate 2,3-dioxygenase (EC 1.13.11.15). This enzyme was active when the bacteria were grown under conditions promoting pigment production. The kinetics and factors affecting pigment production are also reported.