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

Efficient catalytic turnover of cytochrome P450(cam) is supported by a T252N mutation.

Archives of biochemistry and biophysics - 1 Jun 2008

Kim Donghak, Heo Yong-Seok, Ortiz de Montellano Paul R

Abstract excerpt

A Thr (or Ser) residue on the I-helix is a highly conserved structural feature of cytochrome P450 enzymes. It is believed to be indispensable as a proton delivery shuttle in the oxygen activation process. Previous work showed that P450(cin) (CYP176A1), which contains an Asn instead of the conserved Thr, is fully functional in the catalytic oxidation of cineole [D.B. Hawkes, G.W. Adams, A.L. Burlingame, P.R. Ortiz...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to DNA Primers
Share to Gas Chromatography-Mass Spectrometry

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

Share to Hydrogen Peroxide

Share to Hydroxylation

Share to Kinetics

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 18359283
DOI: 10.1016/j.abb.2008.02.044
PMCID: PMC2577879

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

Efficient catalytic turnover of cytochrome P450(cam) is supported by a T252N mutation.PMID 18359283Read ↗

Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism.Semantic proximity Read ↗

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

Quantum mechanical/molecular mechanical calculated reactivity networks reveal how cytochrome P450cam and Its T252A mutant select their oxidation pathways.Semantic proximity Read ↗

The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin.Semantic proximity Read ↗

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.Semantic proximity Read ↗

Redox control of the P450cam catalytic cycle: effects of Y96F active site mutation and binding of a non-natural substrate.Semantic proximity Read ↗

The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM.Semantic proximity Read ↗

L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.Semantic proximity Read ↗

Active site proton delivery and the lyase activity of human CYP17A1.Semantic proximity Read ↗

Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change.Semantic proximity Read ↗

Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1).Semantic proximity Read ↗

Mechanism of the Clinically Relevant E305G Mutation in Human P450 CYP17A1.Semantic proximity Read ↗

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