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

Exploring the Kinetics and Thermodynamics of a Novel Histidine Ammonia-Lyase from Geobacillus kaustophilus.

International journal of molecular sciences - 21 Sept 2024

Salas-Garrucho Francisco Manuel, Carrillo-Moreno Alba, Contreras Lellys M, Rodríguez-Vico Felipe, Clemente-Jiménez Josefa María, Las Heras-Vázquez Francisco Javier

Abstract excerpt

Histidine ammonia-lyase (HAL) plays a pivotal role in the non-oxidative deamination of L-histidine to produce trans-urocanic, a crucial process in amino acid metabolism. This study examines the cloning, purification, and biochemical characterization of a novel HAL from Geobacillus kaustophilus (GkHAL) and eight active site mutants to assess their effects on substrate binding, catalysis, thermostability, and...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to Enzyme Stability

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Substrate Specificity

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 39337646
DOI: 10.3390/ijms251810163
PMCID: PMC11432326

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the Kinetics and Thermodynamics of a Novel Histidine Ammonia-Lyase from Geobacillus kaustophilus.PMID 39337646Read ↗

Functional and structural characterization of thermostable D-amino acid aminotransferases from Geobacillus spp.Semantic proximity Read ↗

Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family.Semantic proximity Read ↗

Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.Semantic proximity Read ↗

Methionine gamma‐lyase: The unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancersSemantic proximity Read ↗

Biochemical insights into the key residue substituents of an L-asparaginase from Thermococcus kodakarensis and their application in acrylamide mitigation.Semantic proximity Read ↗

Discovery and characterization of temperature adaptation modules by mining L-glutamate decarboxylase derived from psychrophilic microorganisms.Semantic proximity Read ↗

Enhancement of glutaminase production through protein design and host strain modification in Bacillus amyloliquefaciens.Semantic proximity Read ↗

Engineered Oxalate decarboxylase boosts activity and stability for biological applicationsSemantic proximity Read ↗

Further characterization and engineering of a 11-amino acid motif for enhancing recombinant protein expressionSemantic proximity Read ↗

Identification of a Novel Cobamide Remodeling Enzyme in the Beneficial Human Gut Bacterium Akkermansia muciniphilaSemantic proximity Read ↗

Significant enhancement of the thermal stability and catalytic efficiency of transglutaminase in Streptomyces mobaraensis engineered through the novel S. mobaraensis genomic mutant library construction method GHR/Sml.Semantic proximity Read ↗

Characterization of Cg10062 from Corynebacterium glutamicum: implications for the evolution of cis-3-chloroacrylic acid dehalogenase activity in the tautomerase superfamily.Semantic proximity Read ↗

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