ArticleJournal of bacteriology2001
Disulfide bond in Pseudomonas aeruginosa lipase stabilizes the structure but is not required for interaction with its foldase.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed, 75 citations in OpenAlex.
- Heterologous expression and foldase-assisted refolding of LipGoM, aBiochemistry and biophysics reports · 2025Article
- Prediction of lipase-specific foldase-dependence in bacterial lipase subfamilies I.1 and I.2.BMC genomics · 2025Article
- Chlorophyllase fromACS bio & med chem Au · 2024Article
- A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds.The Journal of biological chemistry · 2023Article
- N-Acetyl-Cysteine Increases Activity of Peanut-Shaped Gold Nanoparticles Against Biofilms Formed by Clinical Strains ofInfection and drug resistance · 2022Article
- Enhanced Prodigiosin Production inApplied and environmental microbiology · 2021Article
- Functional Heterologous Expression of Mature Lipase LipA fromInternational journal of molecular sciences · 2020Article
- Article
- Cold-active extracellular lipase: Expression in Sf9 insect cells, purification, and catalysis.Biotechnology reports (Amsterdam, Netherlands) · 2019Article
- Production and purification of an alkaline lipase from3 Biotech · 2018Article
- An oxidant and organic solvent tolerant alkaline lipase by P. aeruginosa mutant: downstream processing and biochemical characterization.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2013Article
- Isolation of a thioesterase gene from the metagenome of a mountain peak, Apharwat, in the northwestern Himalayas.3 Biotech · 2013Article
- Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I.1.PloS one · 2012Article
- Purification and characterization of extracellular lipase from a new strain: Pseudomonas aeruginosa SRT 9.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2009Article
- Improved PCR method for the creation of saturation mutagenesis libraries in directed evolution: application to difficult-to-amplify templates.Applied microbiology and biotechnology · 2008Article
- Understanding structural features of microbial lipases--an overview.Analytical chemistry insights · 2008Article
- Hexadecane and Tween 80 stimulate lipase production in Burkholderia glumae by different mechanisms.Applied and environmental microbiology · 2007Article
- DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis.Infection and immunity · 2002Article
- DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa.Journal of bacteriology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa secretes a 29-kDa lipase which is dependent for folding on the presence of the lipase-specific foldase Lif. The lipase contains two cysteine residues which form an intramolecular disulfide bond. Variant lipases with either one or both cysteines replaced by serines showed severely reduced levels of extracellular lipase activity, indicating the importance of the disulfide bond for secretion of lipase through the outer membrane. Wild-type and variant lipase genes fused to the signal sequence of pectate lyase from Erwinia carotovora were expressed in Escherichia coli, denatured by treatment with urea, and subsequently refolded in vitro. Enzymatically active lipase was obtained irrespective of the presence or absence of the disulfide bond, suggesting that the disulfide bond is required neither for correct folding nor for the interaction with the lipase-specific foldase. However, cysteine-to-serine variants were more readily denatured by treatment at elevated temperatures and more susceptible to proteolytic degradation by cell lysates of P. aeruginosa. These results indicate a stabilizing function of the disulfide bond for the active conformation of lipase. This conclusion was supported by the finding that the disulfide bond function could partly be substituted by a salt bridge constructed by changing the two cysteine residues to arginine and aspartate, respectively.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.