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Open and closed states of Candida antarctica lipase B: protonation and the mechanism of interfacial activation.

Stauch B, Fisher SJ, Cianci M
J Lipid Res 56 2348-58 (2015)
Cited: 43 times
EuropePMC logo PMID: 26447231

Abstract

Lipases (EC 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates, such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest also for their industrial applications. The hydrolysis reaction follows a two-step mechanism, or "interfacial activation," with adsorption of the enzyme to a heterogeneous interface and subsequent enhancement of the lipolytic activity. Among lipases, Candida antarctica lipase B (CALB) has never shown any significant interfacial activation, and a closed conformation of CALB has never been reported, leading to the conclusion that its behavior was due to the absence of a lid regulating the access to the active site. The lid open and closed conformations and their protonation states are observed in the crystal structure of CALB at 0.91 Å resolution. Having the open and closed states at atomic resolution allows relating protonation to the conformation, indicating the role of Asp145 and Lys290 in the conformation alteration. The findings explain the lack of interfacial activation of CALB and offer new elements to elucidate this mechanism, with the consequent implications for the catalytic properties and classification of lipases.

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  2. Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues. Matinja AI, Kamarudin NHA, Leow ATC, Oslan SN, Ali MSM. Int J Mol Sci 23 15394 (2022)

Articles - 5a6v mentioned but not cited (5)

  1. Open and closed states of Candida antarctica lipase B: protonation and the mechanism of interfacial activation. Stauch B, Fisher SJ, Cianci M. J Lipid Res 56 2348-2358 (2015)
  2. Machine learning modeling of family wide enzyme-substrate specificity screens. Goldman S, Das R, Yang KK, Coley CW. PLoS Comput Biol 18 e1009853 (2022)
  3. In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters. Azevedo TSM, Silva LKB, Lima ÁS, Pereira MM, Franceschi E, Faria Soares CM. Front Bioeng Biotechnol 9 805059 (2021)
  4. Energetic and Kinetic Origins of CALB Interfacial Activation Revealed by PaCS-MD/MSM. Wijaya TN, Kitao A. J Phys Chem B 127 7431-7441 (2023)
  5. Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B. Jaito N, Kaewsawat N, Phetlum S, Uengwetwanit T. PLoS One 18 e0295397 (2023)


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  3. Enzymatic Remediation of Polyethylene Terephthalate (PET)-Based Polymers for Effective Management of Plastic Wastes: An Overview. Maurya A, Bhattacharya A, Khare SK. Front Bioeng Biotechnol 8 602325 (2020)
  4. Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks. Godoy CA, Pardo-Tamayo JS, Barbosa O. Int J Mol Sci 23 9933 (2022)
  5. An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation. Khairul Anuar NFS, Huyop F, Ur-Rehman G, Abdullah F, Normi YM, Sabullah MK, Abdul Wahab R. Int J Mol Sci 23 12644 (2022)

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