Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Pectate lyase (Pel) plays a crucial role in the maceration of vegetables by soft rot Erwinia spp. We have characterized the four Pel isoenzymes of Erwinia carotovora subspecies carotovora strain SCRI193. In this paper we concentrate on two isoenzymes which have different locations in SCRI193: PLb is periplasmic and PLc is extracellular. Comparison of the gene products and nucleotide sequences of pelB and pelC allowed us to assign them to different gene families. In addition, we have identified a number of conserved amino acid residues that are common to all extracellular Pel isoenzymes.

Original publication

DOI

10.1111/j.1365-2958.1989.tb00164.x

Type

Journal article

Journal

Mol Microbiol

Publication Date

12/1989

Volume

3

Pages

1785 - 1795

Keywords

Amino Acid Sequence, Base Sequence, Enzyme Stability, Erwinia, Escherichia coli, Extracellular Matrix, Genes, Bacterial, Isoenzymes, Molecular Sequence Data, Multigene Family, Polysaccharide-Lyases, Restriction Mapping, Temperature