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

Intragenic complementation and the structure and function of argininosuccinate lyase.

Cellular and molecular life sciences : CMLS - 1 Oct 2000

Yu B, Howell P L

Abstract excerpt

Argininosuccinate lyase (ASL) catalyzes the reversible hydrolysis of argininosuccinate to arginine and fumarate, a reaction important for the detoxification of ammonia via the urea cycle and for arginine biosynthesis. ASL belongs to a superfamily of structurally related enzymes, all of which function as tetramers and catalyze similar reactions in which fumarate is one of the products. Genetic defects in the ASL...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Metabolism, Inborn Errors
Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Genetic Complementation Test

Share to Models, Molecular

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 11092456
DOI: 10.1007/pl00000646
PMCID: PMC11147086

Genes

ASL

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intragenic complementation and the structure and function of argininosuccinate lyase.PMID 11092456Read ↗

Human argininosuccinate lyase: a structural basis for intragenic complementation.Semantic proximity Read ↗

Intragenic complementation at the argininosuccinate lyase locus: reconstruction of the active site.Semantic proximity Read ↗

Intragenic complementation at the human argininosuccinate lyase locus. Identification of the major complementing alleles.Semantic proximity Read ↗

Functional complementation in yeast allows molecular characterization of missense argininosuccinate lyase mutations.Semantic proximity Read ↗

Disruption of a salt bridge dramatically accelerates subunit exchange in duck delta2 crystallin.Semantic proximity Read ↗

Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R.Semantic proximity Read ↗

Mutations and polymorphisms in the human argininosuccinate lyase (ASL) gene.Semantic proximity Read ↗

Understanding the role of argininosuccinate lyase transcript variants in the clinical and biochemical variability of the urea cycle disorder argininosuccinic aciduria.Semantic proximity Read ↗

Molecular analysis of human argininosuccinate lyase: mutant characterization and alternative splicing of the coding region.Semantic proximity Read ↗

Argininosuccinate lyase deficiency: mutational spectrum in Italian patients and identification of a novel ASL pseudogene.Semantic proximity Read ↗

The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.Semantic proximity Read ↗

The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.Semantic proximity Read ↗

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