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

Structure-function relationships in Escherichia coli adenylate cyclase.

The Biochemical journal - 1 Nov 2008

Linder Jürgen U

Abstract excerpt

Class I adenylate cyclases are found in gamma- and delta-proteobacteria. They play central roles in processes such as catabolite repression in Escherichia coli or development of full virulence in pathogens such as Yersinia enterocolitica and Vibrio vulnificus. The catalytic domain (residues 2-446) of the adenylate cyclase of E. coli was overexpressed and purified. It displayed a V(max) of 665 nmol of cAMP x...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Adenylyl Cyclases
Share to Catalysis

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

Share to Escherichia coli Proteins

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Serine

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 18620542
DOI: 10.1042/BJ20080350

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

Structure-function relationships in Escherichia coli adenylate cyclase.PMID 18620542Read ↗

Mutations uncover a role for two magnesium ions in the catalytic mechanism of adenylyl cyclase.Semantic proximity Read ↗

Two-metal-Ion catalysis in adenylyl cyclase.Semantic proximity Read ↗

Mutational and Functional Analyses of Substrate Binding and Catalysis of the Listeria monocytogenes EutT ATP:Co(I)rrinoid Adenosyltransferase.Semantic proximity Read ↗

Crystal structure and functional implication of a bacterial cyclic AMP-AMP-GMP synthetase.Semantic proximity Read ↗

Importance of the region around lysine 196 for catalytic activity of adenylyl cyclase from Escherichia coli.Semantic proximity Read ↗

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state.Semantic proximity Read ↗

Adenylyl cyclase Rv0386 from Mycobacterium tuberculosis H37Rv uses a novel mode for substrate selection.Semantic proximity Read ↗

Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli.Semantic proximity Read ↗

Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.Semantic proximity Read ↗

Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis.Semantic proximity Read ↗

Replenishing the cyclic-di-AMP pool: regulation of diadenylate cyclase activity in bacteria.Semantic proximity Read ↗

Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae.Semantic proximity Read ↗

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