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

Evaluation of Mut(S) and Mut⁺ Pichia pastoris strains for membrane-bound catechol-O-methyltransferase biosynthesis.

Applied biochemistry and biotechnology - 1 Apr 2015

Pedro A Q, Oppolzer D, Bonifácio M J, Maia C J, Queiroz J A, Passarinha L A

Abstract excerpt

Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is an enzyme that catalyzes the methylation of catechol substrates, and while structural and functional studies of its membrane-bound isoform (MBCOMT) are still hampered by low recombinant production, Pichia pastoris has been described as an attractive host for the production of correctly folded and inserted membrane proteins. Hence, in this work, MBCOMT...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Oxidoreductases
Share to Catechol O-Methyltransferase

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

Share to Cell Culture Techniques

Share to Fermentation

Share to Glycerol

Share to Methanol

Share to Pichia

Share to Recombinant Proteins

Source

Identifiers

PMID: 25712908
DOI: 10.1007/s12010-015-1551-0

Genes

COMT

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

Evaluation of Mut(S) and Mut⁺ Pichia pastoris strains for membrane-bound catechol-O-methyltransferase biosynthesis.PMID 25712908Read ↗

Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway.Semantic proximity Read ↗

Genome-scale metabolic reconstruction and in silico analysis of methylotrophic yeast Pichia pastoris for strain improvement.Semantic proximity Read ↗

Pichia pastoris Mut(S) strains are prone to misincorporation of O-methyl-L-homoserine at methionine residues when methanol is used as the sole carbon source.Semantic proximity Read ↗

Production of a sterol esterase from Ophiostoma piceae in batch and fed-batch bioprocesses using different Pichia pastoris phenotypes as cell factory.Semantic proximity Read ↗

Combined use of fluorescent dyes and flow cytometry to quantify the physiological state of Pichia pastoris during the production of heterologous proteins in high-cell-density fed-batch cultures.Semantic proximity Read ↗

Construction and characterization of Pichia pastoris strains for labeling aromatic amino acids in recombinant proteins.Semantic proximity Read ↗

Comparative genomics and transcriptomics of Pichia pastoris.Semantic proximity Read ↗

Implications of evolutionary engineering for growth and recombinant protein production in methanol-based growth media in the yeast Pichia pastoris.Semantic proximity Read ↗

Recombinant protein expression in Pichia pastoris.Semantic proximity Read ↗

High-level production and covalent immobilization of Providencia rettgeri penicillin G acylase (PAC) from recombinant Pichia pastoris for the development of a novel and stable biocatalyst of industrial applicability.Semantic proximity Read ↗

Strategies for optimal synthesis and secretion of heterologous proteins in the methylotrophic yeast Pichia pastoris.Semantic proximity Read ↗

The effect of temperature on the proteome of recombinant Pichia pastoris.Semantic proximity Read ↗

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