Tanaka_2000_J.Biochem_127_597

Reference

Title : Glutathione as an essential factor for chaperon-mediated activation of lactonizing lipase (LipL) from Pseudomonas sp. 109 - Tanaka_2000_J.Biochem_127_597
Author(s) : Tanaka J , Nihira T , Yamada Y
Ref : J Biochem , 127 :597 , 2000
Abstract :

Pseudomonas sp. 109 produces a unique lipase (LipL) which efficiently catalyzes intramolecular transesterification of omega-hydroxyesters to form macrocyclic lactones. The production of the enzymatically active LipL requires a specific molecular chaperon (LimL protein) together with a low-M(r) lipase-activation-factor (LAF) of unknown structure. From 50 g of Pseudomonas cells, 2.15 mg of LAF was purified as a sulfobenzofurazanyl derivative after methanol extraction, derivatization, and C(18) reverse-phase HPLC. One-dimensional and two-dimensional 600 MHz (1)H-NMR and fast atom bombardment mass spectrometry (FAB-MS) revealed that LAF is glutathione. Because several SH compounds (L-cysteine and mercaptoethanol) were similarly effective to native LAF in the activation of LipL, and because only LipL contains two cysteinyl residues forming an intramolecular disulfide bond, it is concluded that the reduction of and reformation of the intramolecular disulfide bond of LipL is essential to liberate free and fully active LipL.

PubMedSearch : Tanaka_2000_J.Biochem_127_597
PubMedID: 10739951
Gene_locus related to this paper: psesp-llipa

Related information

Substrate Glutathione
Gene_locus Glutathione    psesp-llipa
Family Glutathione    psesp-llipa    Bacterial_lip_FamI.1

Citations formats

Tanaka J, Nihira T, Yamada Y (2000)
Glutathione as an essential factor for chaperon-mediated activation of lactonizing lipase (LipL) from Pseudomonas sp. 109
J Biochem 127 :597

Tanaka J, Nihira T, Yamada Y (2000)
J Biochem 127 :597