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

The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant.

Chembiochem : a European journal of chemical biology - 25 Jan 2008

Cryle Max J, De Voss James J

Abstract excerpt

The hydroxylation activity of the Thr268Ala mutant of P450(BM3) has been shown to occur to varying degrees with small alterations in the structure of a fatty-acid substrate. Ten substrates were investigated, including straight chain, branched chain and cis-cyclopropyl substituted fatty acids with a straight-chain length that varied between 12 and 16 carbon atoms. The efficacy of the hydroxylation activity...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Bacillus megaterium
Share to Fatty Acids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydroxylation

Share to Mixed Function Oxygenases

Share to Oxygen

Share to Threonine

Source

Identifiers

PMID: 18161730
DOI: 10.1002/cbic.200700537

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant.PMID 18161730Read ↗

Thr268 in substrate binding and catalysis in P450BM-3.Semantic proximity Read ↗

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.Semantic proximity Read ↗

Mutating a Highly Conserved Residue in Diverse Cytochrome P450s Facilitates Diastereoselective Olefin Cyclopropanation.Semantic proximity Read ↗

Novel haem co-ordination variants of flavocytochrome P450BM3.Semantic proximity Read ↗

A highly active single-mutation variant of P450BM3 (CYP102A1).Semantic proximity Read ↗

Oxygen activation by P450(cin): Protein and substrate mutagenesis.Semantic proximity Read ↗

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.Semantic proximity Read ↗

Oxidative biotransformation of fatty acids by cytochromes P450: predicted key structural elements orchestrating substrate specificity, regioselectivity and catalytic efficiency.Semantic proximity Read ↗

Role of the highly conserved threonine in cytochrome P450 2E1: prevention of H2O2-induced inactivation during electron transfer.Semantic proximity Read ↗

Analysis of the oxidation of short chain alkynes by flavocytochrome P450 BM3.Semantic proximity Read ↗

Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.Semantic proximity Read ↗

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.Semantic proximity Read ↗

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