Article

Structure, Substrate Complexation and Reaction Mechanism of Bacterial Asparaginases

2007-01-01

Abstract excerpt

Asparaginases and glutaminases are enzymes that catalyze the hydrolysis of asparagine or glutamine to the correspondent acid and ammonia. Based on their biochemical properties and sequence homology, this group of proteins, common to various organisms, can be divided into three families: bacterial asparaginases, plant asparaginases and enzymes similar to Rhizobium etli asparaginase. Bacterial L-asparaginases can be...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: d5741654-4b78-58d1-82d5-c1ddd8cebfe0
DOI: 10.2174/2212796810701010075

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Structure, Substrate Complexation and Reaction Mechanism of Bacterial AsparaginasesDOI 10.2174/2212796810701010075Read

Structural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclatureSemantic proximity Read

Structural and biochemical properties of L‐asparaginaseSemantic proximity Read

Mutations in asparaginase II from E. coli and implications for inactivation and PEGylation.Semantic proximity Read

Metagenomic discovery and functional validation of L-asparaginases with anti-leukemic effect from the Caspian SeaSemantic proximity Read

Possible mechanism of metabolic and drug resistance with L-asparaginase therapy in childhood leukaemiaSemantic proximity Read

Desirable L-asparaginases for treating cancer and current research trendsSemantic proximity Read

Elucidation of the Reaction Mechanism of Cavia porcellus l-Asparaginase: A QM/MM Study.Semantic proximity Read

Identification and Structural Analysis of an l-Asparaginase Enzyme from Guinea Pig with Putative Tumor Cell Killing PropertiesSemantic proximity Read

<i>In Silico</i> -Driven Engineering of <i>Halomonas elongata</i> L-Asparaginase: Towards Enhanced Proteolytic Resistance in Lymphoblastic LeukemiaSemantic proximity Read

Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.Semantic proximity Read

Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment.Semantic proximity Read

Comparative immunogenicity and structural analysis of epitopes of different bacterial L-asparaginasesSemantic proximity Read