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

Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.

Journal of molecular biology - 13 Jul 2007

Tsai May, Koo Jason, Yip Patrick, Colman Roberta F, Segall Mark L, Howell P Lynne

Abstract excerpt

Adenylosuccinate lyase (ADL) catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR) to 5-aminoimidazole-4-carboxamide ribotide (AICAR) and fumarate, and of adenylosuccinate (ADS) to adenosine monophosphate (AMP) and fumarate in the de novo purine biosynthetic pathway. ADL belongs to the argininosuccinate lyase (ASL)/fumarase C superfamily of enzymes. Members of this family share...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Escherichia coli

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

Share to ASL gene

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Molecular Structure

Share to Mutation

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 17531264
DOI: 10.1016/j.jmb.2007.04.052
PMCID: PMC4113493

Genes

ASL
C3

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

Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.PMID 17531264Read ↗

Structural and Biochemical Characterization of Human Adenylosuccinate Lyase (ADSL) and the R303C ADSL Deficiency-Associated MutationSemantic proximity Read ↗

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

Mechanistic Insights from the Crystal Structure of Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase Complexed with the Adenylate Intermediate.Semantic proximity Read ↗

Adenylosuccinate lyase deficiency.Semantic proximity Read ↗

Preparation of 5-amino-4-imidazole-N-succinocarboxamide ribotide, 5-amino-4-imidazole-N-succinocarboxamide riboside and succinyladenosine, compounds usable in diagnosis and research of adenylosuccinate lyase deficiency.Semantic proximity Read ↗

Clinical, biochemical and molecular findings in seven Polish patients with adenylosuccinate lyase deficiency.Semantic proximity Read ↗

Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants.Semantic proximity Read ↗

Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.Semantic proximity Read ↗

Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.Semantic proximity Read ↗

The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis.Semantic proximity Read ↗

Structural and functional investigation of the intermolecular interaction between NRPS adenylation and carrier protein domains.Semantic proximity Read ↗

The oxpA5 mutation of Aspergillus nidulans is an allele of adB, the gene encoding adenylosuccinate synthetase.Semantic proximity Read ↗

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