The term chymase is used to signify a chymotrypsin-like protease stored within the secretory granules of mast cells. Primarily based on amino acid sequence homology, 18 chymases have been identified among different animals. This study, which compares the structure of the primary specificity pocket (S1 subsite), defines a subgroup of four chymases likely to have a substrate specificity with more elastase- than chymotrypsin-like qualities. This difference is due, primarily, to finding a Val instead of a Gly at residue 199, a position corresponding to Gly216 in bovine chymotrypsin and Val216 in neutrophil and porcine elastases. Chymases with Val at 199 are found only in animals expressing multiple chymases, consistent with the premise that their substrate specificity differs from that of chymases with Gly at 199.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0014-5793(02)02242-1 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Conserved ancillary residues situated proximally to the VIM-2 active-site affect its metallo β-lactamase activity.
FEMS Microbiol Lett
January 2025
Department of Bioscience and Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur-721302, West Bengal, India.
Verona-integron-metallo-β-lactamase (VIM-2) is one of the most widespread class B β-lactamase responsible for β-lactam resistance. Although active-site residues help in metal binding, the residues nearing the active-site possess functional importance. Here, to decipher the role of such residues in the activity and stability of VIM-2, the residues E146, D182, N210, S207, and D213 were selected through in-silico analyses and substituted with alanine using site-directed mutagenesis.
View Article and Find Full Text PDFMolecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates.
Nat Commun
January 2025
Department of Plant Molecular Biology and Physiology, Albrecht-von-Haller Institute for Plant Sciences, Georg-August-University Göttingen, Julia-Lermontowa-Weg 3, 37077, Göttingen, Germany.
Class I glutaredoxins (GRXs) are nearly ubiquitous proteins that catalyse the glutathione (GSH)-dependent reduction of mainly glutathionylated substrates. In land plants, a third class of GRXs has evolved (class III). Class III GRXs regulate the activity of TGA transcription factors through yet unexplored mechanisms.
View Article and Find Full Text PDFDifferential substrate specificity of ERK, JNK, and p38 MAP kinases toward Connexin 43.
J Biol Chem
January 2025
Department of Biological Sciences, Moravian University, 1200 Main Street, Bethlehem, PA 18018, USA. Electronic address:
Phosphorylation of connexin 43 (Cx43) is an important regulatory mechanism of gap junction (GJ) function. Cx43 is modified by several kinases on over 15 sites within its ∼140 amino acid-long C-terminus (CT). Phosphorylation of Cx43CT on S255, S262, S279, and S282 by ERK has been widely documented in several cell lines, by many investigators.
View Article and Find Full Text PDFPromoted expression of a lipase for its application in EPA/DHA enrichment and mechanistic insights into its substrate specificity.
Int J Biol Macromol
January 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan 430062, PR China. Electronic address:
Expanding toolkits of EPA/DHA enrichment from natural sources is essential for better satisfying increasing demands for them. Lipase K80, from Proteus vulgaris K80, showed an application potential in EPA/DHA enrichment, whereas no desired heterologous expression in generally regarded as safe (GRAS) hosts restricted its relevant applications. In this study, expression of lipase K80 in a well-reputed GRAS host, Pichia pastoris, was achieved and further enhanced via combining disruption of its C-terminal KKL motif with co-expression of N-Acetyltransferase Mpr1, with a cumulative increment of nearly 200 % in the secretion level and the volumetric activity.
View Article and Find Full Text PDFIdentification and Characterization of a New Thermophilic κ-Carrageenan Sulfatase.
J Agric Food Chem
January 2025
Faculty of Chemistry, Biotechnology, and Food Science, NMBU Norwegian University of Life Sciences, P.O. Box 5003, 1432 Aas, Norway.
Carrageenans are sulfated polysaccharides found in the cell wall of certain red seaweeds. They are widely used in the food industry for their gelling and stabilizing properties. In nature, carrageenans undergo enzymatic modification and degradation by marine organisms.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!