Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262.

International journal of biological macromolecules - 1 Jan 2012

Kim Seulgi, Bae Song Yi, Kim Seung Joon, Ngo Tri Duc, Kim Kyeong Kyu, Kim T Doohun

Abstract excerpt

A novel oligomeric hydrolase (LI22) from Listeria innocua CLIP 11262 was identified, characterized, and immobilized for industrial application. Sequence analysis of LI22 revealed a putative catalytic triad (Ser(10)-Asp(176)-His(179)), and a conserved sequence motif Ser(S)(10)-Gly(G)(77)-Asn(N)(79)-His(H)(179) with moderate identities (<30%) with other members of the SGNH-hydrolase superfamily. LI22 was able to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid
Share to Benzothiazoles

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carboxylic Ester Hydrolases

Share to Chromatography, Gel

Share to Cross-Linking Reagents

Share to Listeria

Share to Nitrophenols

Share to Thiazoles

Source

Identifiers

PMID: 22020155
DOI: 10.1016/j.ijbiomac.2011.10.003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization, amyloid formation, and immobilization of a novel SGNH hydrolase from Listeria innocua 11262.PMID 22020155Read ↗

From discovery to potential application: engineering a novel M23 peptidase to combat Listeria monocytogenesSemantic proximity Read ↗

Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triadSemantic proximity Read ↗

Analysis of the peptidoglycan hydrolase complement of Lactobacillus casei and characterization of the major γ-D-glutamyl-L-lysyl-endopeptidase.Semantic proximity Read ↗

Structural and biochemical analyses of β-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila involved in mucin degradation.Semantic proximity Read ↗

Identification of an essential gene responsible for D-Asp incorporation in the Lactococcus lactis peptidoglycan crossbridge.Semantic proximity Read ↗

Directed evolution of a serine protease LsPLAase in Bacillus subtilis for high-yield secretory production and efficient depolymerization of polylactic acid.Semantic proximity Read ↗

Prebiotic Properties of Bacillus Coagulans MA 13: Production of Galactoside Hydrolyzing Enzymes and Characterization of the Transglycosylation Properties of a GH42 β-GalactosidaseSemantic proximity Read ↗

Molecular Characterization of a Novel Family VIII Esterase with β-Lactamase Activity (PsEstA) from Paenibacillus sp.Semantic proximity Read ↗

A novel type of peptidoglycan-binding domain highly specific for amidated D-Asp cross-bridge, identified in Lactobacillus casei bacteriophage endolysins.Semantic proximity Read ↗

Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.Semantic proximity Read ↗

Characterization of a bacterial copper-dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere.Semantic proximity Read ↗

Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.