Characterization Of Two Redundant Aspergillus flavus Peptide Synthetase8208;like Enzymes

Ref ID: 18526

Author:

Daniel Schwenk,
Saori Amaike,
Ry Forseth,
Frank Schroeder,
Nancy Keller,
Dirk Hoffmeister

Author address:

Hans-Knöll-Institut Jena  
University of Wisconsin, Madison, WI  
Cornell University, Ithaca, NY
Friedrich-Schiller-Universität Jena

Full conference title:

11 th European Conference on Fungal Genetics

Abstract:

LaeA, a regulator of secondary metabolism in fungi, controls expression of two genes encoding NRPS8208;like enzymes
in Aspergillus flavus, termed LnaA and LnbA. Although these enzymes resemble α 8208;aminoadipate reductases (i.e.,
primary metabolism enzymes), gene deletion and knockdown experiments pointed to a role for LnaA and LnbA in
secondary metabolism. Specifically, the biosyntheses of heterocyclic L8208;tyrosine8208;derived natural products are
dependent on these enzymes. Genetic data is also suggestive of functional redundancy of these two enzymes.
Hexahistidine8208;tagged LnaA and LnbA were heterologously produced, and assayed using the amino acid8208;dependent
ATP8208;pyrophosphate exchange method.  L8208;tyrosine was identified as clearly preferred substrate of both enzymes.
Further biochemical characterization established divergent temperature and pH8208;optima, and differences regarding
stereospecificity.
Our biochemical experiments prove that the LnaA and LnbA substrate spectrum is compatible with their tentative
heterocyclic products. Further, participation of α 8208;aminoadipate reductase8208;like NRPSs in secondary metabolism and
functional redundancy of LnaA and LnbA, anticipated by genetic methods, is supported by the substrate spectrum
of these enzymes.

Abstract Number: PR8.39

Conference Year: 2012

Link to conference website: http://www.ecfg.info/images/Abstract_Book_Electronic.pdf

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