Open AccessThe protein encoded by the Shewanella colwelliana melA gene is a p ‐hydroxyphenylpyruvate dioxygenase
Author(s) -
Ruzafa Carolina,
Solano Francisco,
SanchezAmat Antonio
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07282.x
Subject(s) - homogentisic acid , dioxygenase , biochemistry , escherichia coli , tyrosine , biology , enzyme , gene , amino acid , gene product , shewanella , chemistry , microbiology and biotechnology , bacteria , gene expression , genetics
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.