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Your search keyword '"Grzegorz M Popowicz"' showing total 2 results
Start Over Author "Grzegorz M Popowicz" Journal chembiochem : a european journal of chemical biology
2 results on '"Grzegorz M Popowicz"'

1. Conversion of a Mono- and Diacylglycerol Lipase into a Triacylglycerol Lipase by Protein Engineering

Author

Grzegorz M. Popowicz, Yonghua Wang, Uwe T. Bornscheuer, Lan Dongming, Pengfei Zhou, and Ioannis V. Pavlidis

Subjects
Models, Molecular, Diacylglycerol lipase, Stereochemistry, In silico, Triacylglycerol lipase, Protein Engineering, Biochemistry, Enzyme catalysis, Substrate Specificity, Catalytic Domain, Point Mutation, Lipase, Molecular Biology, chemistry.chemical_classification, Malassezia, biology, Organic Chemistry, Substrate (chemistry), Protein engineering, Monoacylglycerol Lipases, Lipoprotein Lipase, Enzyme, chemistry, biology.protein, Molecular Medicine
Abstract

Despite the fact that most lipases are believed to be active against triacylglycerides, there is a small group of lipases that are active only on mono- and diacylglycerides. The reason for this difference in substrate scope is not clear. We tried to identify the reasons for this in the lipase from Malassezia globosa. By protein engineering, and with only one mutation, we managed to convert this enzyme into a typical triacylglycerol lipase (the wild-type lipase does not accept triacylglycerides). The variant Q282L accepts a broad spectrum of triacylglycerides, although the catalytic behavior is altered to some extent. From in silico analysis it seems that specific hydrophobic interactions are key to the altered substrate specificity.

Published
2015

2. Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex

Author

Marcin Krajewski, Grzegorz M. Popowicz, Tad A. Holak, and Mahavir Singh

Subjects
Models, Molecular, Protein Denaturation, Protein subunit, Molecular Sequence Data, Crystallography, X-Ray, complex mixtures, Biochemistry, Chromatin remodeling, Protein Structure, Secondary, Histones, Protein structure, Humans, Amino Acid Sequence, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Conserved Sequence, Histone Acetyltransferases, Adenosine Triphosphatases, biology, Circular Dichroism, Lysine, Organic Chemistry, DNA Helicases, Temperature, Nuclear Proteins, Acetylation, SWI/SNF, Bromodomain, Protein Structure, Tertiary, Histone, Mutation, biology.protein, bacteria, Molecular Medicine, Sequence Alignment, Protein Binding, Transcription Factors
Abstract

Bromodomains represent an extensive family of evolutionarily conserved domains that are found in many chromatin-associated proteins such as histone acetyltransferases (HAT) and subunits of ATP-dependent chromatin-remodeling complexes. These domains are associated with acetylated lysine residues that bind both in vivo and in vitro; for example, they bind to the N-acetylated lysines of the histone tail of nucleosomes. In this report, we determined the structure of the bromodomain from human brahma-related gene 1 (BRG1) protein, a subunit of an ATP-dependent switching/sucrose nonfermenting (SWI/SNF) remodeling complex, and have also characterized its in vitro interaction with N-acetylated lysine peptides from histones. In addition to a typical all-alpha-helical fold that was observed in the bromodomains, we observed for the first time a small beta-sheet in the ZA loop region of the BRG1 protein. The BRG1 bromodomain exhibited binding, albeit weak, to acetylated peptides that were derived from histones H3 and H4. We have compared the acetyl-lysine binding sites of BRG1 bromodomain with the yGCN5 (general control of amino acid biosynthesis). By modeling the acetylated-lysine peptide into the BRG1 bromodomain structure, we were able to explain the weak binding of acetylated-lysine peptides to this bromodomain.

Published
2007

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