Cloning and characterization of the gene encoding an esterase from Spirulina platensis.
The gene encoding a 23 kDA serine esterase from the cyanobacterium Spirulina platensis has been identified, cloned, characterized and expressed in Escherichia coli. The primary structure of the esterase deduced from the DNA sequence displayed 32% sequence identity with the carboxylesterase (esterase II) encoded by estB of Pseudomonas fluorescens; the highest degree of homology is found in a stretch of 11 identical or highly conserved amino acid residues corresponding to the GXSXG consensus motif found in the catalytic site of many serine proteases, lipases and esterases.
Salvi
S
S
Department of Biology MCA, University of Camerino, Italy.
Trinei
M
M
Lanfaloni
L
L
Pon
C L
CL
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D000458:Cyanobacteria / Q000201:enzymology / Q000235:genetics*; D004269:DNA, Bacterial; D004950:Esterases / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D004269:DNA, Bacterial; D004950:Esterases; C022635:serine esterase