Evidence map›Paper›PMID 20170513›Full record

ArticleBMC genomics2010

Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A.

Michael Widmann, P Benjamin Juhl, Jürgen Pleiss

Abstract read
In one paragraph

Article in BMC genomics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Production of 4-Ethyl Malate through Position-Specific Hydrolysis ofJournal of microbiology and biotechnology · 2022
    Article
  6. Article
  7. Ethanol as additive enhance the performance of immobilized lipase LipA fromBiotechnology reports (Amsterdam, Netherlands) · 2021
    Article
  8. Increased mRNA Stability and Expression Level ofJournal of microbiology and biotechnology · 2021
    Article
  9. Article
  10. Indoxyl Acetate as a Substrate for Analysis of Lipase Activity.International journal of analytical chemistry · 2019
    Article
  11. Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) fromJournal of biological research (Thessalonike, Greece) · 2018
    Article
  12. Alteration of Chain Length Selectivity ofAdvanced synthesis & catalysis · 2018
    Article
  13. Article
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  15. Review
  16. Article
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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

3 authors.

Michael WidmannInstitute of Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
P Benjamin Juhl
Jürgen Pleiss

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe Lipase Engineering Database (LED) integrates information on sequence, structure and function of lipases, esterases and related proteins with the alpha/beta hydrolase fold. A new superfamily for Candida antarctica lipase A (CALA) was introduced including the recently published crystal structure of CALA. Since CALA has a highly divergent sequence in comparison to other alpha/beta hydrolases, the Lipase Engineering Database was used to classify CALA in the frame of the already established classification system. This involved the comparison of CALA to similar structures as well as sequence-based comparisons against the content of the LED.

resultsThe new release 3.0 (December 2009) of the Lipase Engineering Database contains 24783 sequence entries for 18585 proteins as well as 656 experimentally determined protein structures, including the structure of CALA. In comparison to the previous release 1 with 4322 protein and 167 structure entries this update represents a significant increase in data volume. By comparing CALA to representative structures from all superfamilies, a structure from the deacetylase superfamily was found to be most similar to the structure of CALA. While the alpha/beta hydrolase fold is conserved in both proteins, the major difference is found in the cap region. Sequence alignments between both proteins show a sequence similarity of only 15%. A multisequence alignment of both protein families was used to create hidden Markov models for the cap region of CALA and showed that the cap region of CALA is unique among all other proteins of the alpha/beta hydrolase fold. By specifically comparing the substrate binding pocket of CALA to other binding pockets of alpha/beta hydrolases, the binding pocket of Candida rugosa lipase was identified as being highly similar. This similarity also applied to the lid of Candida rugosa lipase in comparison to the potential lid of CALA.

conclusionThe LED serves as a valuable tool for the systematic analysis of single proteins or protein families. The updated release 3.0 was used for the evaluation of alpha/beta hydrolases. The HTML version of the database with new features is available at http://www.led.uni-stuttgart.de and provides sequences, structures and a set of analysis tools including phylogenetic trees and HMM profiles.

Indexed as

Databases, ProteinAmino Acid SequenceCandidaLipaseMarkov ChainsModels, MolecularMolecular Sequence DataProtein Structure, TertiarySequence AlignmentSequence Analysis, ProteinSoftwareLipase

Identifiers

PMID20170513
PMCPMC2841678

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.