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

Exploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.

Biochemistry - 8 Jul 2014

Buller Andrew R, Freeman Michael F, Schildbach Joel F, Townsend Craig A

Abstract excerpt

In the past decade, there have been major achievements in understanding the relationship between enzyme catalysis and protein structural plasticity. In autoprocessing systems, however, there is a sparsity of direct evidence of the role of conformational dynamics, which are complicated by their intrinsic chemical reactivity. ThnT is an autoproteolytically activated enzyme involved in the biosynthesis of the...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Proteolysis

Share to Thienamycins

Source

Open in PubMed Open full text

Identifiers

PMID: 24933323
DOI: 10.1021/bi500385d
PMCID: PMC4095933

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.PMID 24933323Read ↗

Evolution of conformational dynamics determines the conversion of a promiscuous generalist into a specialist enzyme.Semantic proximity Read ↗

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase.Semantic proximity Read ↗

The mechanism of autocatalytic activation of plant-type L-asparaginases.Semantic proximity Read ↗

Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.Semantic proximity Read ↗

Probing the enzymatic activity and maturation process of the EcAIII Ntn-amidohydrolase using local random mutagenesis.Semantic proximity Read ↗

Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.Semantic proximity Read ↗

A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis.Semantic proximity Read ↗

Protein tolerance to random circular permutation correlates with thermostability and local energetics of residue-residue contacts.Semantic proximity Read ↗

The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology.Semantic proximity Read ↗

Dynamic allostery in substrate binding by human thymidylate synthaseSemantic proximity Read ↗

Understanding the autocatalytic process of pro-kumamolisin activation from molecular dynamics and quantum mechanical/molecular mechanical (QM/MM) free-energy simulations.Semantic proximity Read ↗

Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymes.Semantic proximity Read ↗

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