Results 21 to 30 of about 68,716 (153)

Genome-Wide Identification, Evolution, and Expression of GDSL-Type Esterase/Lipase Gene Family in Soybean

open access: yesFrontiers in Plant Science, 2020
GDSL-type esterase/lipase proteins (GELPs) belong to the SGNH hydrolase superfamily and contain a conserved GDSL motif at their N-terminus. GELPs are widely distributed in nature, from microbes to plants, and play crucial roles in growth and development,
Hong-Gang Su   +11 more
doaj   +2 more sources

Evaluation of the Structure-Function Relationship of SGNH Lipase from Streptomyces rimosus by Site-Directed Mutagenesis and Computational Approach. [PDF]

open access: yesInt J Mol Sci
Streptomyces rimosus extracellular lipase (SrL) is a multifunctional hydrolase belonging to the SGNH family. Here site-directed mutagenesis (SDM) was used for the first time to investigate the functional significance of the conserved amino acid residues ...
Filić Ž   +7 more
europepmc   +2 more sources

Visualization of a substrate-induced productive conformation of the catalytic triad of theNeisseria meningitidispeptidoglycanO-acetylesterase reveals mechanistic conservation in SGNH esterase family members

open access: yesActa Crystallographica Section D: Biological Crystallography, 2014
Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors.
Bertrand Raynal   +2 more
exaly   +2 more sources

Functional domains of Acinetobacter bacteriophage tail fibers. [PDF]

open access: yesFront Microbiol
A rapid increase in antimicrobial resistant bacterial infections around the world is causing a global health crisis. The Gram-negative bacterium Acinetobacter baumannii is categorized as a Priority 1 pathogen for research and development of new ...
Peters DL, Gaudreault F, Chen W.
europepmc   +3 more sources

Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15 [PDF]

open access: yesInternational Journal of Biological Macromolecules, 2018
GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively ...
Jonet, Mohd Anuar   +5 more
core   +2 more sources

Bioinformatics approach to characterization of SGNH/GDSL-hydrolases [PDF]

open access: yesActa Crystallographica Section A Foundations of Crystallography, 2005
Biserka Koji ć -Prodi ć   +5 more
semanticscholar   +2 more sources

Non-targeted metabonomics and transcriptomics revealed the mechanism of mulberry branch extracts promoting the growth of Sanghuangporus vaninii mycelium

open access: yesFrontiers in Microbiology, 2022
Sanghuangprous vaninii is a wood-inhabiting fungus, and its mycelium and fruiting body show excellent medicinal values. Mulberry is one of the major hosts of S. vaninii, however, the mechanism of mulberry affecting the growth of S.
Jinxi Huo   +7 more
doaj   +1 more source

Understanding the structure and function of GDSL-type esterase/lipase genes in pigeon pea for their role under moisture stress conditions

open access: yesPlant Stress, 2023
The SGNH hydrolase superfamily's GDSL-type esterase/lipase proteins (GELPs) play a crucial role in plant growth and stress tolerance. However, limited knowledge exists regarding the molecular role of GELP genes under drought conditions, especially in ...
Suman Pahal   +5 more
doaj   +1 more source

Uncharacterized DUF1574 leptospira proteins are SGNH hydrolases [PDF]

open access: yesCell Cycle, 2008
Leptospira borgpetersenii and Leptospira interrogans are nonsporulating bacteria responsible for leptospirosis, which is presumed to be the most widespread zoonosis in the world. This water-borne pathogen is usually transmitted to humans through the contact with contaminated soil or water, via infected animal tissue or rat bites. Consequently, farmers,
Lukasz, Knizewski   +7 more
openaire   +2 more sources

Biochemical Characterization of Multimodular Xylanolytic Carbohydrate Esterases from the Marine Bacterium Flavimarina sp. Hel_I_48. [PDF]

open access: yesChembiochem
Multimodular carbohydrate‐active enzymes often combine different catalytic activities for efficient polysaccharide degradation. In this work, the structural and functional characterization of three multimodular xylan‐targeting esterases, Fl6, Fll1 and Fll4 from Flavimarina sp. Hel_I_48, are presented.
Teune M   +4 more
europepmc   +2 more sources

Home - About - Disclaimer - Privacy