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

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.

15 Aug 1995

Abstract excerpt

Using partial amino acid sequence data derived from porcine methionyl aminopeptidase (MetAP; methionine aminopeptidase, peptidase M; EC 3.4.11.18), a full-length clone of the homologous human enzyme has been obtained. The cDNA sequence contains 2569 nt with a single open reading frame corresponding to a protein of 478 amino acids. The C-terminal portion representing the catalytic domain shows limited identity...

Read the complete abstract on PubMed

Topics

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

Share to Biochemical and Molecular Research
Share to Cancer Research and Treatments
Share to Peptidase Inhibition and Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 7644482
DOI: 10.1073/pnas.92.17.7714

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes.PMID 7644482Read ↗

Advances in Bacterial Methionine Aminopeptidase InhibitionSemantic proximity Read ↗

Methionine aminopeptidases and angiogenesisSemantic proximity Read ↗

Mammalian mitochondrial intermediate peptidase: structure/function analysis of a new homologue from Schizophyllum commune and relationship to thimet oligopeptidases.Semantic proximity Read ↗

A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2.Semantic proximity Read ↗

Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit.Semantic proximity Read ↗

Identification of critical residues in the active site of porcine membrane-bound aminopeptidase P.Semantic proximity Read ↗

An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway.Semantic proximity Read ↗

Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A.Semantic proximity Read ↗

The Methionyl Aminopeptidase from <i>Escherichia coli</i> Can Function as an Iron(II) EnzymeSemantic proximity Read ↗

MtpB, a member of the MttB superfamily from the human intestinal acetogen Eubacterium limosum, catalyzes proline betaine demethylationSemantic proximity Read ↗

Acquisition of new function through gene duplication in the metallocarboxypeptidase familySemantic proximity Read ↗

Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase familiesSemantic proximity Read ↗

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