The protein encoded by the Shewanella colwelliana melA gene is a p-hydroxyphenylpyruvate dioxygenase.
The identity of the product of the melA 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-hydroxyphenyl-pyruvate 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.
Ruzafa
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C
Department of Biochemistry, School of Medicine, University of Murcia, Spain.
Solano
F
F
Sanchez-Amat
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A
D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000235:genetics* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001419:Bacteria / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D015111:4-Hydroxyphenylpyruvate Dioxygenase