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

Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity.

Biotechnology letters - 1 Apr 2011

Wu Xiao-Bin, Tian Xiu-Yun, Ji Jun-Jie, Wu Wei-Bin, Fan Ke-Qiang, Yang Ke-Qian

Abstract excerpt

Deacetoxy/deacetylcephalosporin C synthase (acDAOC/DACS) from Acremonium chrysogenum is a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C. The R308 residue located in close proxim...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, High Pressure Liquid
Share to Mutagenesis
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidoreductases

Share to Penicillin G

Share to Substrate Specificity

Source

Identifiers

PMID: 21190060
DOI: 10.1007/s10529-010-0504-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21190060-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity.PMID 21190060Read ↗

C-terminus mutations of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase with improved activity toward penicillin analogs.Semantic proximity Read ↗

Controlling the substrate selectivity of deacetoxycephalosporin/deacetylcephalosporin C synthase.Semantic proximity Read ↗

Relevant double mutations in bioengineered Streptomyces clavuligerus deacetoxycephalosporin C synthase result in higher binding specificities which improve penicillin bioconversion.Semantic proximity Read ↗

Mutation of N304 to leucine in Streptomyces clavuligerus deacetoxycephalosporin C synthase creates an enzyme with increased penicillin analogue conversion.Semantic proximity Read ↗

Active site mutations of recombinant deacetoxycephalosporin C synthase.Semantic proximity Read ↗

Iterative combinatorial mutagenesis as an effective strategy for generation of deacetoxycephalosporin C synthase with improved activity toward penicillin G.Semantic proximity Read ↗

Expanding Aminoglycoside Resistance Enzyme Regiospecificity by Mutation and Truncation.Semantic proximity Read ↗

Analysis of the Effect of N555 Mutations on the Product Specificity of Dextransucrase Using Caffeic Acid Phenethyl Ester as an Acceptor Substrate.Semantic proximity Read ↗

Engineered hydrophobic pocket of (S)-selective arylmalonate decarboxylase variant by simultaneous saturation mutagenesis to improve catalytic performance.Semantic proximity Read ↗

Characterization of the inserted mutagenesis dextransucrases from Leuconostoc mesenteroides 0326 to produce hyperbranched dextran.Semantic proximity Read ↗

Overexpression of synthesized cephalosporin C acylase containing mutations in the substrate transport tunnel.Semantic proximity Read ↗

Mutational analysis of a key residue in the substrate specificity of a cephalosporin acylase.Semantic proximity Read ↗

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