RT Journal Article SR Electronic(1) A1 Tanaka, Junko A1 Ihara, Fumio A1 Nihira, Takuya A1 Yamada, Yasuhiro YR 1999 T1 A low-Mr lipase activation factor cooperating with lipase modulator protein LimL in Pseudomonas sp. strain 109 JF Microbiology, VO 145 IS 10 SP 2875 OP 2880 DO https://doi.org/10.1099/00221287-145-10-2875 PB Microbiology Society, SN 1465-2080, AB Pseudomonas sp. strain 109 produces a unique lipase (LipL) which efficiently catalyses intramolecular transesterification of ω-hydroxyesters to form macrocyclic lactones. In vivo production of enzymically active LipL requires lipase modulator protein (LimL), which functions as a molecular chaperone for the correct folding of LipL. However, previous work has shown that LipL forms a tight complex with LimL in vitro and the resulting LipL–LimL complex is only partially active, suggesting an additional mechanism that facilitates the dissociation of the complex to form enzymically active LipL. In the present work, a low-M r compound (lipase activation factor, LAF) was found in Pseudomonas sp. strain 109 that when added to the LipL–LimL complex resulted in the activation of LipL. Ca2+ ions also enhanced lipase activity, but the instantaneous activation by Ca2+ was different from the gradual and time-dependent activation by LAF, indicating the novel nature of this compound. LAF passed through an ultrafiltration membrane with an M r cut-off of 3000 and showed an apparent M r of 330±30 on Superdex Peptide gel-filtration chromatography. Treatment of the LipL–LimL complex with LAF liberated free active LipL, indicating that LAF was necessary to dissociate the LipL–LimL complex., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-145-10-2875