Structural and functional insights into the enzymatic activities of lipases from Burkholderia stagnalis and Burkholderia plantarii.
Burkholderia
crystal structure
interesterification activity
kinetics
lipase
protein engineering
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
24 Apr 2024
24 Apr 2024
Historique:
revised:
13
03
2024
received:
07
02
2024
accepted:
19
03
2024
medline:
25
4
2024
pubmed:
25
4
2024
entrez:
24
4
2024
Statut:
aheadofprint
Résumé
Lipases with high interesterification activity are important enzymes for industrial use. The lipase from Burkholderia stagnalis (BsL) exhibits higher interesterification activity than that from Burkholderia plantarii (BpL) despite their significant sequence similarity. In this study, we determined the crystal structure of BsL at 1.40 Å resolution. Utilizing structural insights, we have successfully augmented the interesterification activity of BpL by over twofold. This enhancement was achieved by substituting threonine with serine at position 289 through forming an expansive space in the substrate-binding site. Additionally, we discuss the activity mechanism based on the kinetic parameters. Our study sheds light on the structural determinants of the interesterification activity of lipase.
Identifiants
pubmed: 38658173
doi: 10.1002/1873-3468.14883
doi:
Banques de données
RefSeq
['WP_059565995', 'WP_042628289', 'WP_059963281', 'WP_055140564']
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2024 Federation of European Biochemical Societies.
Références
Guo Y, Cai Z, Xie Y, Ma A, Zhang H, Rao P and Wang Q (2020) Synthesis, physicochemical properties, and health aspects of structured lipids: a review. Compr Rev Food Sci Food Saf 19, 759–800.
Casas‐Godoy L, Gasteazoro F, Duquesne S, Bordes F, Marty A and Sandoval G (2018) Lipases: an overview. Methods Mol Biol 1835, 3–38.
Fjerbaek L, Christensen KV and Norddahl B (2009) A review of the current state of biodiesel production using enzymatic transesterification. Biotechnol Bioeng 102, 1298–1315.
Lai OM, Ghazali HM, Cho F and Chong CL (2000) Enzymatic transesterification of palm stearin: anhydrous milk fat mixtures using 1, 3‐specific and non‐specific lipases. Food Chem 70, 221–225.
Nardini M, Lang DA, Liebeton K, Jaeger KE and Dijkstra BW (2000) Crystal structure of Pseudomonas aeruginosa lipase in the open conformation: the prototype for family I. 1 of bacterial lipases. J Biol Chem 275, 31219–31225.
Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD et al. (1997) The open conformation of a Pseudomonas lipase. Structure 5, 187–202.
Noble MEM, Cleasby A, Johnson LN, Egmond MR and Frenken LGJ (1993) The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett 331, 123–128.
Khan FI, Lan D, Durrani R, Huan W, Zhao Z and Wang Y (2017) The lid domain in lipases: structural and functional determinant of enzymatic properties. Front Bioeng Biotechnol 5, 16.
Lang DA, Mannesse ML, De Haas GH, Verheij HM and Dijkstra BW (1998) Structural basis of the chiral selectivity of Pseudomonas cepacia lipase. Eur J Biochem 254, 333–340.
Kataoka S, Kawamoto S, Tsumura K and Ishikawa K (2023) Comparison of enzymatic activities of lipases from Burkholderia plantarii and Burkholderia cepacia. Arch Microbiol 205, 309.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Lambré C, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lampi E, Mengelers M et al. (2023) Safety evaluation of the food enzyme triacylglycerol lipase from the non‐genetically modified Burkholderia stagnalis strain PL266‐QLM. EFSA J 21, e07907.
El Khattabi M, Van Gelder P, Bitter W and Tommassen J (2000) Role of the lipase‐specific foldase of Burkholderia glumae as a steric chaperone. J Biol Chem 275, 26885–26891.
Rosenau F, Tommassen J and Jaeger KE (2004) Lipase‐specific foldases. Chembiochem 5, 152–161.
Otwinowski Z and Minor W (1997) Processing of X‐ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307–326.
McCoy AJ, Grosse‐Kunstleve RW, Adams PD, Winn MD, Storoni LC and Read RJ (2007) Phaser crystallographic software. J Appl Cryst 40, 658–674.
Project CC (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50 (Pt 5), 760–763.
Emsley P and Cowtan K (2004) Coot: model‐building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126–2132.
Murshudov GN, Vagin AA and Dodson EJ (1997) Refinement of macromolecular structures by the maximum‐likelihood method. Acta Crystallogr D Biol Crystallogr 53, 240–255.
Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33, 491–497.
Winn MD, Ballard CC, Cowtan KD, Dodson EJ, Emsley P, Evans PR, Keegan RM, Krissinel EB, Leslie AG, McCoy A et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67, 235–242.
DeLano WL (2002) Pymol: an open‐source molecular graphics tool. CCP4 Newsl Protein Crystallogr 40, 82–92.
Fukatsu M, Thorsteinson CT, Daun JK and Tamura T (1997) Determination of lipase activity by high performance liquid chromatography. J Oleo Sci 46, 697–700.
Lewis DR and Liu DJ (2012) Direct measurement of lipase inhibition by orlistat using a dissolution linked in vitro assay. Clin Pharmacol Biopharm 1, 103.
Sakoda M and Hiromi K (1976) Determination of the best‐fit values of kinetic parameters of the Michaelis‐Menten equation by the method of least squares with the Taylor expansion. J Biochem 80, 547–555.
Korman TP and Bowie JU (2012) Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I. 1. PLoS One 7, e52890.
El Khattabi M, Van Gelder P, Bitter W and Tommassen J (2003) Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase. J Mol Catal B: Enzym 22, 329–338.