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

Characterization of the Pro101Gln mutation that enhances the catalytic performance of T. indicus NADH-dependent d-lactate dehydrogenase.

Structure (London, England : 1993) - 7 Dec 2023

Liu Jiongqin, Liu Gongquan, Han Xiao, Tao Fei, Xu Ping

Abstract excerpt

NADH-dependent d-lactate dehydrogenases (d-LDH) are important for the industrial production of d-lactic acid. Here, we identify and characterize an improved d-lactate dehydrogenase mutant (d-LDH1) that contains the Pro101Gln mutation. The specific enzyme activities of d-LDH1 toward pyruvate and NADH are 21.8- and 11.0-fold greater compared to the wild-type enzyme. We determined the crystal structure of Apo-d-LDH1...

Read the complete abstract on PubMed

Topics

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

Share to L-Lactate Dehydrogenase
Share to Lactic Acid

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

Share to Mutation

Source

Identifiers

PMID: 37729918
DOI: 10.1016/j.str.2023.08.019

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

Characterization of the Pro101Gln mutation that enhances the catalytic performance of T. indicus NADH-dependent d-lactate dehydrogenase.PMID 37729918Read ↗

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of L-lactate dehydrogenase and its H171C mutant from Bacillus subtilis.Semantic proximity Read ↗

Directed modification of l-LcLDH1, an l-lactate dehydrogenase from Lactobacillus casei, to improve its specific activity and catalytic efficiency towards phenylpyruvic acid.Semantic proximity Read ↗

The catalytic action of human d-lactate dehydrogenase is severely inhibited by oxalate and is impaired by mutations triggering d-lactate acidosis.Semantic proximity Read ↗

Efficient production of enantiomerically pure D-phenyllactate from phenylpyruvate by structure-guided design of an engineered D-lactate dehydrogenase.Semantic proximity Read ↗

Distinct conformation-mediated functions of an active site loop in the catalytic reactions of NAD-dependent D-lactate dehydrogenase and formate dehydrogenase.Semantic proximity Read ↗

The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.Semantic proximity Read ↗

Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.Semantic proximity Read ↗

A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli.Semantic proximity Read ↗

Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase.Semantic proximity Read ↗

Altered Cofactor Preference of Thermostable StDAPDH by a Single Mutation at K159.Semantic proximity Read ↗

Positive selection on D-lactate dehydrogenases of Lactobacillus delbrueckii subspecies bulgaricus.Semantic proximity Read ↗

An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.Semantic proximity Read ↗

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