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Title

 

 

 

 

Phylogenetic analysis of homologous fatty acid synthase and polyketide synthase involved in aflatoxin biosynthesis

 

Authors

Marina Marcet-Houben1, Maria Cabré2, José L. Paternáin2 and Antoni Romeu2, *

 

Affiliation

1Department of Bioinformatics, Centro de Investigación Principe felipe, E-46013 Valencia, Spain; 2Department of Biochemistry and Biotechnology, University Rovira i Virgili, E-43007 Tarragona, Spain

 

Email

antoni.romeu@urv.cat; *Corresponding author

 

Article Type

Hypothesis

 

Date

received May 24, 2008; accepted August 31, 2008; published  September 20, 2008

 

Abstract

The first two steps of aflatoxin biosynthesis are catalyzed by the HexA/B and by the Pks protein. The phylogenetic analysis clearly distinguished fungal HexA/B from FAS subunits and from other homologous proteins. The phylogenetic trees of the HexA and HexB set of proteins share the same clustering. Proteins involved in the synthesis of fatty acids or in the aflatoxin or sterigmatocystin biosynthesis cluster separately. The Pks phylogenetic tree also differentiates the aflatoxin-related polypeptide sequences from those of other kinds of secondary metabolism. The function of some of the A. flavus Pks homologues may be deduced from the phylogenetic analysis. The conserved sequence motifs of protein domains shared by HexA/B and Pks - namely, β-polyketide synthase (KS), acetyl transferase (AT) and acyl carrier protein (ACP) - have been identified, and the HexA/B and Pks involved in aflatoxin biosynthesis have been distinguished from those involved in primary metabolism or other kinds of secondary metabolism.

 

Keywords

aflatoxin; aflatoxin biosynthesis; HexA/B multienzymatic complex; polyketide synthase; Aspergillus

 

Citation

Marcet-Houben et al., Bioinformation 3(1): 33-40 (2008)

 

Edited by

P. Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

 

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.