Tyrosine 2-hydroxylation by <i>Aeromonas salmonicida</i>

Morgan, John G.; McGettigan, Seán; Donlon, John

doi:10.1042/bst0130464

Cited by 3 publications

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“…Melanin in A. salmonicida ssp. salmonicida is formed by oxidation and polymerization steps of tyrosine ( Morgan, McGettigan & Donlon 1985). In the SVLT‐1, ‐2, ‐5 and ‐6 isolates, the lack of ability to produce melanin following incubation on medium enriched with tyrosine could result from mutations in or deletions of genes controlling the melanin pathway, as described in certain fungi ( Bell, Puhalla, Tolmsoff & Stipanovic 1976; Geis, Wheeler & Staniszlo 1984), but also from expression disturbances of the melanin pathway enzymes ( Sanchez‐Amat, Ruzafa & Solano 1998).…”

Section: Discussionmentioning

confidence: 99%

Non‐pigment‐producing isolates of Aeromonas salmonicida subspecies salmonicida: isolation, identification, transmission and pathogenicity in Atlantic salmon, Salmo salar L.

Koppang¹,

Fjølstad

Melgård³

et al. 2000

Journal of Fish Diseases

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Four non‐pigment‐producing isolates and two pigment‐producing isolates of Aeromonas salmonicida sp. salmonicida were isolated from the head‐kidney of diseased farmed Atlantic salmon, Salmo salar L. The cultural, morphological and biochemical features of the isolates were compared with those of reference strains. Injection and cohabitation experiments were performed. The only difference between the non‐pigment‐producing isolates and the pigment producing reference strains of A. salmonicida ssp. salmonicida was the inability of the former to produce pigment. In the injection experiments, the investigated non‐pigment‐producing isolate produced a significantly higher mortality compared with the mortality caused by the reference strain, whereas no difference in mortality was detected in the cohabitation experiments.

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Section: Discussionmentioning

confidence: 99%

Non‐pigment‐producing isolates of Aeromonas salmonicida subspecies salmonicida: isolation, identification, transmission and pathogenicity in Atlantic salmon, Salmo salar L.

Koppang¹,

Fjølstad

Melgård³

et al. 2000

Journal of Fish Diseases

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“…The pigments formed by Serratia marcescens through the 3,4-dihydroxyacetate pathway [8] and the pyomelanins produced by Pseudomonas aeruginosa [9] belong to that type of melanin-like pigments. In Aeromonas salmonicida, a novel enzymatic activity responsible for melanin biosynthesis has been described, which is able to catalyse L-tyrosine hydroxylation at position 2 [10]. Shewanella colwelliana is a marine bacterium that produces a dark brown pigment [11].…”

Section: Introductionmentioning

confidence: 99%

The protein encoded by the Shewanella colwelliana melA gene is a p-hydroxyphenylpyruvate dioxygenase

Ruzafa¹

1994

FEMS Microbiology Letters

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The identity of the product of the meL4 gene from Shewanella colwelliana with the enzyme p-hydroxyphenylpyruvic dioxygenase is shown. Cloning of the melA gene endowed Escherichia coli with the capacity to synthesize melanin-like pigments from L-tyrosine. E. coli contained transaminases that transforms L-tyrosine into p-hydroxyphenylpyruvate. This keto acid was detected in the cultures. On the other hand, E. coli containing melA was able to go further in the catabolic pathway, releasing a great amount of homogentisic acid. This acid can spontaneously polymerize giving the pigment. Furthermore, p-hydroxyphenylpyruvate dioxygenase activity was detected in this system. Analysis of the deduced amino acid sequence revealed a high homology with the p-hydroxyphenylpyruvate dioxygenase enzyme from different organisms.

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The protein encoded by the Shewanella colwellianamelA gene is a p-hydroxyphenylpyruvate dioxygenase

Ruzafa

Solano

Sánchez-Amat

1994

FEMS Microbiology Letters

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The identity of the product of the melA gene from Shewanella colelliana with the enzyme p‐hydroxyphenylpyruvic dioxygenase is shown. Cloning of the melA gene endowed Escherichia coli with the capacity to synthesize melanin‐like pigments from L‐tyrosine. E. coli contained transaminases that transforms L‐tyrosine into p‐hydroxyphenylpyruvate. This keto acid was detected in the cultures. On the other hand, E. coli containing melA was able to go further in the catabolic pathway, releasing a great amount of homogentisic acid. This acid can spontaneously polymerize giving the pigment. Furthermore, p‐hydroxyphenylpyruvate dioxygenase activity was detected in this system. Analysis of the deduced amino acid sequence revealed a high homology with the p‐hydroxyphenylpyruvate deoxygenase enzyme from different organisms.

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Tyrosine 2-hydroxylation by Aeromonas salmonicida

Cited by 3 publications

References 0 publications

Non‐pigment‐producing isolates of Aeromonas salmonicida subspecies salmonicida: isolation, identification, transmission and pathogenicity in Atlantic salmon, Salmo salar L.

Non‐pigment‐producing isolates of Aeromonas salmonicida subspecies salmonicida: isolation, identification, transmission and pathogenicity in Atlantic salmon, Salmo salar L.

The protein encoded by the Shewanella colwelliana melA gene is a p-hydroxyphenylpyruvate dioxygenase

The protein encoded by the Shewanella colwellianamelA gene is a p-hydroxyphenylpyruvate dioxygenase

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