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Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis.

ABSTRACT: A candidate for a vaccine against infectious bovine keratoconjunctivitis (IBK) has been cloned and characterized from Moraxella bovis. The plb gene encodes a protein of 616 amino acids (molecular mass of ~65.8 kDa) that expresses phospholipase B activity. Amino acid sequence analysis revealed that PLB is a new member of the GDSL (Gly-Asp-Ser-Leu) family of lipolytic enzymes.

SUBMITTER: Farn JL

PROVIDER: S-EPMC95508 | biostudies-literature | 2001 Nov

REPOSITORIES: biostudies-literature

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Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis.

Farn J L JL Strugnell R A RA Hoyne P A PA Michalski W P WP Tennent J M JM

Journal of bacteriology 20011101 22

A candidate for a vaccine against infectious bovine keratoconjunctivitis (IBK) has been cloned and characterized from Moraxella bovis. The plb gene encodes a protein of 616 amino acids (molecular mass of ~65.8 kDa) that expresses phospholipase B activity. Amino acid sequence analysis revealed that PLB is a new member of the GDSL (Gly-Asp-Ser-Leu) family of lipolytic enzymes. ...[more]

PMID: 11673447

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