Evidence map›Paper›PMID 22492397›Full record

ArticleProtein science : a publication of the Protein Society2012

SABER: a computational method for identifying active sites for new reactions.

Geoffrey R Nosrati, K N Houk

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Computational tools for the evaluation of laboratory-engineered biocatalysts.Chemical communications (Cambridge, England) · 2016
    Review
  4. Article
  5. Article
  6. Computational strategies for the design of new enzymatic functions.Archives of biochemistry and biophysics · 2015
    Review
  7. Article
  8. Article
  9. Article
  10. Recent advances in rational approaches for enzyme engineering.Computational and structural biotechnology journal · 2012
    Review
  11. Computational Enzyme Design: Advances, hurdles and possible ways forward.Computational and structural biotechnology journal · 2012
    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

2 authors at 1 institution in 1 country.

Geoffrey R NosratiDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-1569, USA.
K N Houk
University of California, Los Angeles · US

Funding

CHEMISTRY BIOLOGY INTERFACE TRAINING PROGRAMT32GM008496 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MAYNARD, HEATHER D · 1993 to 2019
$6.3M
Design of New Enzyme CatalystsR01GM075962 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HOUK, KENDALL N · 2009 to 2012
$1.2M
NIGMS NIH HHS GM 75962NIGMS NIH HHS T32 GM008496-16
6 · The paper itself

Abstract

A software suite, SABER (Selection of Active/Binding sites for Enzyme Redesign), has been developed for the analysis of atomic geometries in protein structures, using a geometric hashing algorithm (Barker and Thornton, Bioinformatics 2003;19:1644-1649). SABER is used to explore the Protein Data Bank (PDB) to locate proteins with a specific 3D arrangement of catalytic groups to identify active sites that might be redesigned to catalyze new reactions. As a proof-of-principle test, SABER was used to identify enzymes that have the same catalytic group arrangement present in o-succinyl benzoate synthase (OSBS). Among the highest-scoring scaffolds identified by the SABER search for enzymes with the same catalytic group arrangement as OSBS were L-Ala D/L-Glu epimerase (AEE) and muconate lactonizing enzyme II (MLE), both of which have been redesigned to become effective OSBS catalysts, demonstrated by experiments. Next, we used SABER to search for naturally existing active sites in the PDB with catalytic groups similar to those present in the designed Kemp elimination enzyme KE07. From over 2000 geometric matches to the KE07 active site, SABER identified 23 matches that corresponded to residues from known active sites. The best of these matches, with a 0.28 Å catalytic atom RMSD to KE07, was then redesigned to be compatible with the Kemp elimination using RosettaDesign. We also used SABER to search for potential Kemp eliminases using a theozyme predicted to provide a greater rate acceleration than the active site of KE07, and used Rosetta to create a design based on the proteins identified.

Indexed as

AlgorithmsCatalytic DomainSoftwareComputational BiologyDatabases, ProteinEnzymesModels, MolecularProtein ConformationProtein EngineeringEnzymes

Identifiers

PMID22492397
PMCPMC3403467
OpenAlexW2144958064

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.