The putative lipase, AF1763, from Archaeoglobus fulgidusis is a carboxylesterase with a very high pH optimum.
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.
Rusnak
Monika
M
Institute for Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.
Nieveler
Jens
J
Schmid
Rolf D
RD
Petri
Ralf
R
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
D019843:Archaeal Proteins; D011994:Recombinant Proteins; D043182:Carboxylesterase; D008049:Lipase