title: The putative lipase, AF1763, from Archaeoglobus fulgidusis is a carboxylesterase with a very high pH optimum.
abstract: The open reading frame AF1763, annotated as a putative lipase gene (lipA) of the hyperthermophilic archaeon, Archaeoglobus fulgidus DSM 4304, was cloned and over-expressed in E. coli. A sequence analysis of LipA and the investigation of a truncated enzyme implied a special function of the C-terminal part of LipA. The substrate spectrum of the enzyme suggested that LipA is a carboxylesterase rather than a canonical lipase. The enzyme showed optimal activity at 70 degrees C and between pH 10 and 11, which is among the most alkaline pH range detected for hydrolases.
authors.affiliation: Institute for Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
authors.forename: Monika
authors.initials: M
authors.lastname: Rusnak
authors.forename: Jens
authors.initials: J
authors.lastname: Nieveler
authors.forename: Rolf D
authors.initials: RD
authors.lastname: Schmid
authors.forename: Ralf
authors.initials: R
authors.lastname: Petri
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D019609:Archaeoglobus / Q000201:enzymology*; D043182:Carboxylesterase / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids / Q000235:genetics; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D043182:Carboxylesterase; D008049:Lipase