(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Pseudomonadales: NE > Pseudomonadaceae: NE > Pseudomonas: NE > Pseudomonas aeruginosa group: NE > Pseudomonas mendocina: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide 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.) Pseudomonas mendocina ymp: N, E.
Pseudomonas mendocina EGD-AQ5: N, E.
Pseudomonas mendocina DLHK: N, E.
Pseudomonas mendocina NK-01: N, E.
Pseudomonas mendocina S5.2: N, E.
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 MKKNKTLLALCLGTGLLASGQTQAFWFGSSGYTQTKYPIVLGHGMLGFDS ILGVDYWYGIPAALRRDGASVYVTEVSQLDTSEARGEQLLQQVEDIVAIS GKGKVNLIGHSHGGPTTRYVAAVRPDLVASVTSVGAPHKGSATADFLKGI SEGPAGPVATPVLVGIVNGLGALINFLSGSSSTTPQNALGSLESLNSEGA ARFNAKFPQGIPTSACGEGAYSVNGVRYYSWSGTSPLTNVLDPSDLLLGA SSLTFGSEANDGLVGRCSSRMGQVIRDNYRMNHLDEVNQTLGLTSLFETD PVTVYRQHANRLKNAGL
Reference
Title: Two Extracellular Poly(sigma-caprolactone)-Degrading Enzymes From Pseudomonas hydrolytica sp. DSWY01(T): Purification, Characterization, and Gene Analysis Li L, Lin X, Bao J, Xia H, Li F Ref: Front Bioeng Biotechnol, 10:835847, 2022 : PubMed
Poly(sigma-caprolactone) (PCL) is an artificial polyester with commercially promising application. In this study, two novel PCL-degrading enzymes named PCLase I and PCLase II were purified to homogeneity from the culture supernatant of an effective polyester-degrading bacterium, Pseudomonas hydrolytica sp. DSWY01(T). The molecular masses of PCLase I and PCLase II were determined to be 27.5 and 30.0 kDa, respectively. The optimum temperatures for the enzyme activities were 50 and 40 degreesC, and the optimum pH values were 9.0 and 10.0, respectively. The two enzymes exhibited different physical and chemical properties, but both enzymes could degrade PCL substrates into monomers and oligomers. Weight loss detection and scanning electron microscopy revealed that PCLase I had more effective degradation ability than PCLase II. The genes of the two enzymes were cloned on the basis of the peptide fingerprint analysis results. The sequence analysis and substrate specificity analysis results showed that PCLase I and PCLase II were cutinase and lipase, respectively. Interface activation experiment also confirmed this conclusion. Structural analysis and modeling were further performed to obtain possible insights on the mechanism.
Pseudomonas mendocina lipase PmCut PCLase I