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

Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation.

Journal of molecular biology - 8 Dec 2000

Hehir M J, Murphy J E, Kantrowitz E R

Abstract excerpt

Escherichia coli alkaline phosphatase (EC 3.1.3.1) belongs to a rare group of enzymes that exhibit intragenic complementation. When certain mutant versions of alkaline phosphatase are combined, the resulting heterodimeric enzymes exhibit a higher level of activity than would be expected based upon the relative activities of the parental enzymes. Nine previously identified alkaline phosphatase complementation...

Read the complete abstract on PubMed

Topics

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

Share to Alkaline Phosphatase
Share to Dimerization
Share to Holoenzymes

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

Share to Magnesium

Share to Protein Structure, Quaternary

Share to Protein Subunits

Share to Static Electricity

Source

Identifiers

PMID: 11099386
DOI: 10.1006/jmbi.2000.4230

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

Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation.PMID 11099386Read ↗

Identification of four unique clones encoding 10 kDa proteins from Bacillus that cause phenotypic complementation of a phoA mutant strain of Escherichia coli.Semantic proximity Read ↗

In vitro and in vivo complementation of the Helicobacter pylori arginase mutant using an intergenic chromosomal site.Semantic proximity Read ↗

Towards a model to explain the intragenic complementation in the heteromultimeric protein propionyl-CoA carboxylase.Semantic proximity Read ↗

Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.Semantic proximity Read ↗

Correlation between catalytic efficiency and the transcription read-out in chemical complementation: a general assay for enzyme catalysis.Semantic proximity Read ↗

Subunit complementation of Escherichia coli adenylosuccinate synthetase.Semantic proximity Read ↗

Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure.Semantic proximity Read ↗

Functional analysis of the nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT) enzyme, involved in the late steps of coenzyme B12 biosynthesis in Salmonella enterica.Semantic proximity Read ↗

Function assignment to conserved residues in mammalian alkaline phosphatases.Semantic proximity Read ↗

A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.Semantic proximity Read ↗

Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.Semantic proximity Read ↗

Functional testing of putative oligopeptide permease (Opp) proteins of Borrelia burgdorferi: a complementation model in opp− Escherichia coliSemantic proximity Read ↗

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