Isolation and structure of the pectin lyase D-encoding gene from Aspergillus niger.

The filamentous fungus, Aspergillus niger, produces a number of extracellular pectin-degrading enzymes. We present here the isolation and the complete nucleotide sequence of the gene, pelD, coding for a pectin lyase D (PLD), which was previously described as pectin lyase I (Van Houdenhoven, Ph.D. Thesis, Wageningen, 1975). The deduced amino acid (aa) sequence corresponds to 373 aa residues including a signal peptide of 19 aa. The coding region is interrupted by four short introns (57-65 bp). The nucleotide sequence of the 5'- and 3'-flanking regions is also presented and shows no unusual features. By comparing the deduced aa sequences of the A. niger PLD and a number of bacterial pectate lyases, short regions of homology were found despite the different substrate specificities (high methoxyl-pectin versus low methoxyl-pectin or polygalacturonate) of these enzymes.