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

Effect of Active Site Pocket Structure Modification of D-Stereospecific Amidohydrolase on the Recognition of Stereospecific and Hydrophobic Substrates.

Molecular biotechnology - 1 Sept 2018

Elyas Yasmeen Yousif Ahmed, Miyatani Kazusa, Shimizu Katsuhiko, Arima Jiro

Abstract excerpt

D-Stereospecific amidohydrolase (DAH) from Streptomyces sp. 82F2 has potential utility for the synthesis of D/L configuration dipeptides by an aminolysis reaction. Structural comparison of DAH with substrate-bound D-amino acid amidase revealed that three residues located in the active site pocket of DAH (Thr145, Ala267, and Gly271) might be involved in interactions with D-phenylalanine substrate. We substituted...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Amidohydrolases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Hydrolysis

Share to Hydrophobic and Hydrophilic Interactions

Share to Phenylalanine

Share to Stereoisomerism

Share to Substrate Specificity

Source

Identifiers

PMID: 30051300
DOI: 10.1007/s12033-018-0104-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of Active Site Pocket Structure Modification of D-Stereospecific Amidohydrolase on the Recognition of Stereospecific and Hydrophobic Substrates.PMID 30051300Read ↗

Single-Cell-Based Screening and Engineering of d-Amino Acid Amidohydrolases Using Artificial Amidophenol Substrates and Microbial Biosensors.Semantic proximity Read ↗

Change in substrate preference of Streptomyces aminopeptidase through modification of the environment around the substrate binding site.Semantic proximity Read ↗

Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution.Semantic proximity Read ↗

I86A/C295A mutant secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus has broadened substrate specificity for aryl ketones.Semantic proximity Read ↗

On the catalytic mechanism and stereospecificity of Escherichia coli L-threonine aldolase.Semantic proximity Read ↗

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

Using directed evolution to probe the substrate specificity of mandelamide hydrolase.Semantic proximity Read ↗

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

L-allo-threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.Semantic proximity Read ↗

Characterization of mutants of Sulfolobus solfataricus signature amidase able to hydrolyse R-ketoprofen amide.Semantic proximity Read ↗

Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine dehydrogenase from Thermoactinomyces intermedius.Semantic proximity Read ↗

Discrimination of aliphatic substrates by a single amino acid substitution in Bacillus badius and Bacillus sphaericus phenylalanine dehydrogenases.Semantic proximity Read ↗

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