Has a broad substrate specificity. Hydrolyzes various p-nitrophenyl phosphates, aromatic esters and p-nitrophenyl fatty acids in vitro. Most active against paraoxon, phenyl acetate and p-nitrophenyl caproate (C6), respectively. Has also tributyrinase activity, but shows no hydrolytic activity toward other triacylglycerols including tricaprylin, trimyristin, tripalmitin or triolein in vitro.
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Archaea: NE > TACK group: NE > Crenarchaeota: NE > Thermoprotei: NE > Sulfolobales: NE > Sulfolobaceae: NE > Sulfolobus: NE > Sulfolobus acidocaldarius: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Sulfolobus acidocaldarius DSM 639: N, E.
Sulfolobus acidocaldarius Ron12/I: N, E.
Sulfolobus acidocaldarius N8: N, E.
Sulfolobus acidocaldarius SUSAZ: N, E.
Saccharolobus solfataricus: N, E.
Sulfolobus solfataricus: N, E.
Sulfolobus solfataricus 98/2: N, E.
Sulfolobus solfataricus P2: N, E.
Molecular evidence
Database
No mutation 1 structure: 5L2P: Crystal structure of Sulfolobus solfataricus esterase/lipase Arylesterase No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MPLDPEVRNFLQVYYKANIIDFTKYQFQEIRQKVNELLAKAVPKDPVGET RDMKIKLEDYELPIRIYSPIKRTNNGLVMHFHGGAWILGSIETEDAISRI LSNSCECTVISVDYRLAPEYKFPTAVYDCFNAIVWARDNAGELGIDKDKI ATFGISAGGNLVAATSLLARDNKLKLTAQVPVVPFVYLDLASKSMNRYRK GYFLDINLPVDYGVKMYIRDEKDLYNPLFSPLIAEDLSNLPQAIVVTAEY DPLRDQGEAYAYRLMESGVPTLSFRVNGNVHAFLGSPRTSRQVTVMIGAL LKDIFK
References
Title: A novel thermostable arylesterase from the archaeon Sulfolobus solfataricus P1: purification, characterization, and expression Park YJ, Yoon SJ, Lee HB Ref: Journal of Bacteriology, 190:8086, 2008 : PubMed
A novel thermostable arylesterase, a 35-kDa monomeric enzyme, was purified from the thermoacidophilic archaeon Sulfolobus solfataricus P1. The optimum temperature and pH were 94 degrees C and 7.0, respectively. The enzyme displayed remarkable thermostability: it retained 52% of its activity after 50 h of incubation at 90 degrees C. In addition, the purified enzyme showed high stability against denaturing agents, including various detergents, urea, and organic solvents. The enzyme has broad substrate specificity besides showing an arylesterase activity toward aromatic esters: it exhibits not only carboxylesterase activity toward tributyrin and p-nitrophenyl esters containing unsubstituted fatty acids from butyrate (C(4)) to palmitate (C(16)), but also paraoxonase activity toward organophosphates such as p-nitrophenylphosphate, paraoxon, and methylparaoxon. The k(cat)/K(m) ratios of the enzyme for phenyl acetate and paraoxon, the two most preferable substrates among all tested, were 30.6 and 119.4 s(-1) microM(-1), respectively. The arylesterase gene consists of 918 bp corresponding to 306 amino acid residues. The deduced amino acid sequence shares 34% identity with that of arylesterase from Acinetobacter sp. strain ADP1. Furthermore, we successfully expressed active recombinant S. solfataricus arylesterase in Escherichia coli. Together, our results show that the enzyme is a serine esterase belonging to the A-esterases and contains a catalytic triad composed of Ser156, Asp251, and His281 in the active site.
Sulfolobus acidocaldarius is an aerobic thermoacidophilic crenarchaeon which grows optimally at 80 degrees C and pH 2 in terrestrial solfataric springs. Here, we describe the genome sequence of strain DSM639, which has been used for many seminal studies on archaeal and crenarchaeal biology. The circular genome carries 2,225,959 bp (37% G+C) with 2,292 predicted protein-encoding genes. Many of the smaller genes were identified for the first time on the basis of comparison of three Sulfolobus genome sequences. Of the protein-coding genes, 305 are exclusive to S. acidocaldarius and 866 are specific to the Sulfolobus genus. Moreover, 82 genes for untranslated RNAs were identified and annotated. Owing to the probable absence of active autonomous and nonautonomous mobile elements, the genome stability and organization of S. acidocaldarius differ radically from those of Sulfolobus solfataricus and Sulfolobus tokodaii. The S. acidocaldarius genome contains an integrated, and probably encaptured, pARN-type conjugative plasmid which may facilitate intercellular chromosomal gene exchange in S. acidocaldarius. Moreover, it contains genes for a characteristic restriction modification system, a UV damage excision repair system, thermopsin, and an aromatic ring dioxygenase, all of which are absent from genomes of other Sulfolobus species. However, it lacks genes for some of their sugar transporters, consistent with it growing on a more limited range of carbon sources. These results, together with the many newly identified protein-coding genes for Sulfolobus, are incorporated into a public Sulfolobus database which can be accessed at http://dac.molbio.ku.dk/dbs/Sulfolobus.
Sulfolobus acidocaldarius Sulfolobus solfataricus esterase/lipase Arylesterase
