Evidence map›Paper›PMID 21710970›Full record

ArticleBiochemistry2011

Water in the active site of ketosteroid isomerase.

Philip Hanoian, Sharon Hammes-Schiffer

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Thermodynamic framework for identifying free energy inventories of enzyme catalytic cycles.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  3. Article
  4. Article
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.

Philip HanoianDepartment of Chemistry, 104 Chemistry Building, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Sharon Hammes-Schiffer
Pennsylvania State University · US

Funding

Simulation of Proton and Hydride Transfer in EnzymesR37GM056207 · NIGMS · YALE UNIVERSITY · PI HAMMES-SCHIFFER, SHARON · 2011 to 2020
$3.2M
SIMULATION OF PROTON AND HYDRIDE TRANSFER IN ENZYMESR01GM056207 · NIGMS · UNIVERSITY OF NOTRE DAME · PI HAMMES-SCHIFFER, SHARON · 1998 to 2010
$2.7M
NIGMS NIH HHS GM56207NIGMS NIH HHS R01 GM056207NIGMS NIH HHS R37 GM056207
6 · The paper itself

Abstract

Classical molecular dynamics simulations were utilized to investigate the structural and dynamical properties of water in the active site of ketosteroid isomerase (KSI) to provide insight into the role of these water molecules in the enzyme-catalyzed reaction. This reaction is thought to proceed via a dienolate intermediate that is stabilized by hydrogen bonding with residues Tyr16 and Asp103. A comparative study was performed for the wild-type (WT) KSI and the Y16F, Y16S, and Y16F/Y32F/Y57F (FFF) mutants. These systems were studied with three different bound ligands: equilenin, which is an intermediate analog, and the intermediate states of two steroid substrates. Several distinct water occupation sites were identified in the active site of KSI for the WT and mutant systems. Three additional sites were identified in the Y16S mutant that were not occupied in WT KSI or the other mutants studied. The number of water molecules directly hydrogen bonded to the ligand oxygen was approximately two in the Y16S mutant and one in the Y16F and FFF mutants, with intermittent hydrogen bonding of one water molecule in WT KSI. The molecular dynamics trajectories of the Y16F and FFF mutants reproduced the small conformational changes of residue 16 observed in the crystal structures of these two mutants. Quantum mechanical/molecular mechanical calculations of (1)H NMR chemical shifts of the protons in the active site hydrogen-bonding network suggest that the presence of water in the active site does not prevent the formation of short hydrogen bonds with far-downfield chemical shifts. The molecular dynamics simulations indicate that the active site water molecules exchange much more frequently for WT KSI and the FFF mutant than for the Y16F and Y16S mutants. This difference is most likely due to the hydrogen-bonding interaction between Tyr57 and an active site water molecule that is persistent in the Y16F and Y16S mutants but absent in the FFF mutant and significantly less probable in WT KSI.

Indexed as

CatalysisCatalytic DomainCrystallography, X-RayHydrogen BondingKetosteroidsMolecular Dynamics SimulationMutagenesis, Site-DirectedProteobacteriaPseudomonas putidaStereoisomerismSteroid IsomerasesStructure-Activity RelationshipSubstrate SpecificityTyrosineWaterKetosteroidssteroid delta-isomeraseSteroid IsomerasesTyrosineWater

Identifiers

PMID21710970
PMCPMC3149774
OpenAlexW2042520306

What OpenQuestion holds

Textmetadata
LicenceTDM
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.