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

Altered Cofactor Preference of Thermostable StDAPDH by a Single Mutation at K159.

International journal of molecular sciences - 5 Mar 2020

Gao Xiuzhen, Ma Qinyuan, Song Huihui, Sun Xinming, Li Zhiyun, Liu Mingfei

Abstract excerpt

D-amino acid production from 2-keto acid by reductive amination is an attractive pathway because of its high yield and environmental safety. StDAPDH, a meso-diaminopimelate dehydrogenase (meso-DAPDH) from Symbiobacterium thermophilum, was the first meso-DAPDH to show amination of 2-keto acids. Furthermore, StDAPDH shows excellent thermostability compared to other meso-DAPDHs. However, the cofactor of StDAPDH is...

Read the complete abstract on PubMed

Topics

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

Share to NADP
Share to Actinobacteria
Share to Amino Acid Oxidoreductases

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

Share to Binding Sites

Share to Protein Conformation

Share to Substrate Specificity

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 32150965
DOI: 10.3390/ijms21051788
PMCID: PMC7084900

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

Altered Cofactor Preference of Thermostable StDAPDH by a Single Mutation at K159.PMID 32150965Read ↗

Structural and mutational studies on the unusual substrate specificity of meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum.Semantic proximity Read ↗

[Effect of residue Y76 on co-enzyme specificity of meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum].Semantic proximity Read ↗

Engineering the cofactor specificity of an alcohol dehydrogenase via single mutations or insertions distal to the 2'-phosphate group of NADP(H).Semantic proximity Read ↗

Creation of bioorthogonal redox systems depending on nicotinamide flucytosine dinucleotide.Semantic proximity Read ↗

Engineering Escherichia coli Nicotinic Acid Mononucleotide Adenylyltransferase for Fully Active Amidated NAD Biosynthesis.Semantic proximity Read ↗

Structural analysis reveals the substrate-binding mechanism for the expanded substrate specificity of mutant meso-diaminopimelate dehydrogenase.Semantic proximity Read ↗

High-Throughput Screening of Coenzyme Preference Change of Thermophilic 6-Phosphogluconate Dehydrogenase from NADP(+) to NAD(.).Semantic proximity Read ↗

Engineering d-Lactate Dehydrogenase to Favor an Non-natural Cofactor Nicotinamide Cytosine Dinucleotide.Semantic proximity Read ↗

Kinetic characterization and structural modeling of an NADP+-dependent succinic semialdehyde dehydrogenase from Anabaena sp. PCC7120.Semantic proximity Read ↗

Structural and Biochemical Insights into Dimethylsulfoniopropionate Cleavage by Cofactor-Bound DddK from the Prolific Marine Bacterium Pelagibacter.Semantic proximity Read ↗

3,6-Anhydro-L-Galactose Dehydrogenase VvAHGD is a Member of a New Aldehyde Dehydrogenase Family and Catalyzes by a Novel Mechanism with Conformational Switch of Two Catalytic Residues Cysteine 282 and Glutamate 248.Semantic proximity Read ↗

The β2αB loop determines NAD(P) cofactor specificity and kinetics in trypanosomal D-3-hydroxybutyrate dehydrogenases.Semantic proximity Read ↗

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