The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity

Microbiology (Reading). 2000 Jul;146 ( Pt 7):1585-1591. doi: 10.1099/00221287-146-7-1585.

Abstract

The Bacillus pumilus gene encoding acetyl xylan esterase (axe) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) purified from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar size and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylesterase / biosynthesis
  • Acetylesterase / chemistry
  • Acetylesterase / genetics*
  • Amino Acid Sequence
  • Bacillus / enzymology
  • Bacillus / genetics*
  • Bacteria, Anaerobic / enzymology
  • Bacteria, Anaerobic / genetics
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Genetic Vectors
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Sequence Alignment
  • Substrate Specificity

Substances

  • Recombinant Proteins
  • Carboxylic Ester Hydrolases
  • cephalosporin-C deacetylase
  • Acetylesterase
  • acetylxylan esterase

Associated data

  • GENBANK/AJ249957