Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of conserved Met112 residue in the catalytic activity and stability of ketosteroid isomerase.

Biochimica et biophysica acta - 1 Oct 2016

Cha Hyung Jin, Jang Do Soo, Jeong Jae-Hee, Hong Bee Hak, Yun Young Sung, Shin Eun Ju, Choi Kwan Yong

Abstract excerpt

Ketosteroid isomerase (3-oxosteroid Δ(5)-Δ(4)-isomerase, KSI) from Pseudomonas putida catalyzes allylic rearrangement of the 5,6-double bond of Δ(5)-3-ketosteroid to 4,5-position by stereospecific intramolecular transfer of a proton. The active site of KSI is formed by several hydrophobic residues and three catalytic residues (Tyr14, Asp38, and Asp99). In this study, we investigated the role of a hydrophobic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Hydrophobic and Hydrophilic Interactions

Share to Methionine

Share to Pseudomonas putida

Share to Steroid Isomerases

Share to Transition Temperature

Source

Identifiers

PMID: 27375051
DOI: 10.1016/j.bbapap.2016.06.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of conserved Met112 residue in the catalytic activity and stability of ketosteroid isomerase.PMID 27375051Read ↗

Maintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Contribution of a low-barrier hydrogen bond to catalysis is not significant in ketosteroid isomerase.Semantic proximity Read ↗

The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.Semantic proximity Read ↗

Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Determining the catalytic role of remote substrate binding interactions in ketosteroid isomerase.Semantic proximity Read ↗

Impact of mutation on proton transfer reactions in ketosteroid isomerase: insights from molecular dynamics simulations.Semantic proximity Read ↗

Rescue of deleterious mutations by the compensatory Y30F mutation in ketosteroid isomerase.Semantic proximity Read ↗

Crystal structure of N-domain of FKBP22 from Shewanella sp. SIB1: dimer dissociation by disruption of Val-Leu knot.Semantic proximity Read ↗

Evaluating the catalytic contribution from the oxyanion hole in ketosteroid isomerase.Semantic proximity Read ↗

Contribution of the hydrogen-bond network involving a tyrosine triad in the active site to the structure and function of a highly proficient ketosteroid isomerase from Pseudomonas putida biotype B.Semantic proximity Read ↗

Role of polar and nonpolar residues at the active site for PPIase activity of FKBP22 from Shewanella sp. SIB1.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.