Evidence map›Paper›PMID 17379142›Full record

ArticleChemistry & biology2007

Diversification of catalytic function in a synthetic family of chimeric cytochrome p450s.

Marco Landwehr, Martina Carbone, Christopher R Otey, Yougen Li, Frances H Arnold

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
12.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 71 citations in OpenAlex.

  1. Cytochrome P450The Journal of biological chemistry · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
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  7. Article
  8. Navigating the protein fitness landscape with Gaussian processes.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Recent advances in rational approaches for enzyme engineering.Computational and structural biotechnology journal · 2012
    Review
  11. Article
  12. Exploring protein fitness landscapes by directed evolution.Nature reviews. Molecular cell biology · 2009
    Review
  13. Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. In the light of directed evolution: pathways of adaptive protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Review
  16. Review
  17. Expanding the repertoire of biofuel alternatives through metabolic pathway evolution.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Marco LandwehrDivision of Chemistry and Chemical Engineering, California Institute of Technology, Mail Code 210-41, Pasadena, CA 91125, USA.
Martina Carbone
Christopher R Otey
Yougen Li
Frances H Arnold
California Institute of Technology · US

Funding

Synthetic Protein Families by Structure-Guided SCHEMA RecombinationR01GM068664 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI ARNOLD, FRANCES H · 2003 to 2010
$1.7M
NIGMS NIH HHS GM068664-0NIGMS NIH HHS R01 GM068664
6 · The paper itself

Abstract

We report initial characterization of a synthetic family of more than 3000 cytochrome P450s made by SCHEMA recombination of 3 bacterial CYP102s. A total of 16 heme domains and their holoenzyme fusions with each of the 3 parental reductase domains were tested for activity on 11 different substrates. The results show that the chimeric enzymes have acquired significant functional diversity, including the ability to accept substrates not accepted by the parent enzymes. K-means clustering analysis of the activity data allowed the enzymes to be classified into five distinct groups based on substrate specificity. The substrates can also be grouped such that one can be a "surrogate" for others in the group. Fusion of a functional chimeric heme domain with a parental reductase domain always reconstituted a functional holoenzyme, indicating that key interdomain interactions are conserved upon reductase swapping.

Indexed as

Bacterial ProteinsCatalysisCloning, MolecularCluster AnalysisConserved SequenceCytochrome P-450 Enzyme SystemEscherichia coliGenetic VariationKineticsRecombinant Fusion ProteinsBacterial ProteinsCytochrome P-450 Enzyme SystemRecombinant Fusion Proteins

Identifiers

PMID17379142
PMCPMC1991292
OpenAlexW2103213776

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.