Evidence map›Paper›PMID 17996718›Full record

ArticleArchives of biochemistry and biophysics2008

Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif.

L Sangeetha Vedula, Jiaoyang Jiang, Tatiana Zakharian, David E Cane, David W Christianson

Abstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 79 citations in OpenAlex.

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  16. Traversing the fungal terpenome.Natural product reports · 2014
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  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

L Sangeetha VedulaRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.
Jiaoyang Jiang
Tatiana Zakharian
David E Cane
David W Christianson
University of Pennsylvania · USBrown University · US

Funding

STRUCTURE/FUNCTION OF BIOSYNTHETIC ENZYMESR01GM056838 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI CHRISTIANSON, DAVID W · 1998 to 2025
$8.0M
STEREOCHEMICAL STUDIES OF ISOPRENOID BIOSYNTHESISR01GM030301 · NIGMS · BROWN UNIVERSITY · PI CANE, DAVID E · 1985 to 2015
$5.4M
STEROCHEMICAL STUDIES 0F ISOPRENOID BIOSYNTHESISR37GM030301 · NIGMS · BROWN UNIVERSITY · PI CANE, DAVID E · 1994 to 2003
$1.8M
NIGMS NIH HHS R01 GM030301NIGMS NIH HHS R01 GM056838NIGMS NIH HHS R37 GM030301
6 · The paper itself

Abstract

Trichodiene synthase from Fusarium sporotrichioides contains two metal ion-binding motifs required for the cyclization of farnesyl diphosphate: the "aspartate-rich" motif D(100)DXX(D/E) that coordinates to Mg2+A and Mg2+C, and the "NSE/DTE" motif N(225)DXXSXXXE that chelates Mg2+B (boldface indicates metal ion ligands). Here, we report steady-state kinetic parameters, product array analyses, and X-ray crystal structures of trichodiene synthase mutants in which the fungal NSE motif is progressively converted into a plant-like DDXXTXXXE motif, resulting in a degradation in both steady-state kinetic parameters and product specificity. Each catalytically active mutant generates a different distribution of sesquiterpene products, and three newly detected sesquiterpenes are identified. In addition, the kinetic and structural properties of the Y295F mutant of trichodiene synthase were found to be similar to those of the wild-type enzyme, thereby ruling out a proposed role for Y295 in catalysis.

Indexed as

Amino Acid MotifsAsparagineBiochemistryCarbon-Carbon LyasesCatalytic DomainCrystallography, X-RayEscherichia coliFusariumGlutamic AcidKineticsMagnesiumModels, ChemicalMutagenesis, Site-DirectedSerineTyrosineAsparagineCarbon-Carbon LyasesGlutamic AcidMagnesiumSerinetrichodiene synthetaseTyrosine

Identifiers

PMID17996718
PMCPMC2329581
OpenAlexW2024305976

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.