A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases.
A fragment of genomic DNA from Sulfolobus acidocaldarius DSM 639 encoding a lipolytic enzyme was cloned and sequenced. The 314-amino acid polypeptide displays a maximum sequence similarity (43%) to a putative polyhydroxyalkanoate depolymerase from Pseudomonas oleovorans and contains the pentapeptide G-X1-S-X2-G which is typical of serine hydrolases. The protein is highly thermostable and is able to hydrolyse a variety of lipid substrates thus providing a promising tool for potential biotechnological applications.
Arpigny
J L
JL
Lehrstuhl für Biologie der Mikroorganismen, Ruhr-Universität Bochum, Germany. jeanlouis.arpigny@ruhr-uni-bochum.de
Jendrossek
D
D
Jaeger
K E
KE
D000595:Amino Acid Sequence; D002265:Carboxylic Ester Hydrolases / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D019641:DNA, Archaeal / Q000235:genetics; D004795:Enzyme Stability; D004950:Esterases / Q000235:genetics* / Q000378:metabolism; D019766:Genes, Archaeal; D006358:Hot Temperature; D008066:Lipolysis; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D016945:Sulfolobus acidocaldarius / Q000201:enzymology* / Q000235:genetics*
D019641:DNA, Archaeal; D004950:Esterases; D002265:Carboxylic Ester Hydrolases; C077226:poly(3-hydroxyalkanoic acid) depolymerase