title: Characterization of the Erwinia carotovora peh gene and its product polygalacturonase.
abstract: The peh gene, encoding polygalacturonase (Peh), was identified in Erwinia carotovora strain EC and cloned in Escherichia coli. Recombinant Peh (re-Peh) was purified from E. coli strain 706 containing peh on a recombinant plasmid. The activity of the re-Peh protein is optimal at pH 5.5. The N-terminal and internal amino acid (aa) sequences of re-Peh were determined and compared to the aa sequence deduced from the nucleotide (nt) sequence of the cloned peh. The re-Peh has no similarity, based on either the nt sequences or the deduced aa sequences, to pectate lyases from the same Er. carotovora strain or other organisms.
authors.affiliation: Department of Microbiology, University of California, Los Angeles 90021.
authors.forename: S P
authors.initials: SP
authors.lastname: Lei
authors.forename: H C
authors.initials: HC
authors.lastname: Lin
authors.forename: S S
authors.initials: SS
authors.lastname: Wang
authors.forename: P
authors.initials: P
authors.lastname: Higaki
authors.forename: G
authors.initials: G
authors.lastname: Wilcox
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D016973:Pectobacterium carotovorum / Q000201:enzymology / Q000235:genetics*; D010957:Plasmids; D011096:Polygalacturonase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D004269:DNA, Bacterial; D011994:Recombinant Proteins; D011096:Polygalacturonase