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

Structure and characterization of a NAD(P)H-dependent carbonyl reductase from Pseudomonas aeruginosa PAO1.

FEBS letters - 1 Jun 2017

Li Shanshan, Teng Xiaozhen, Su Li, Mao Guannan, Xu Yueyang, Li Tingting, Liu Riuhua, Zhang Qionglin, Wang Yingying, Bartlam Mark

Abstract excerpt

To investigate the function of the pa4079 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1, we determined its crystal structure and confirmed it to be a NAD(P)-dependent short-chain dehydrogenase/reductase. Structural similarity and activity for a broad range of substrates indicate that PA4079 functions as a carbonyl reductase. Comparison of apo- and holo-PA4079 shows that NADP stabilizes the...

Read the complete abstract on PubMed

Topics

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

Share to Aldehyde Reductase
Share to Apoenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Enzyme Stability

Share to Holoenzymes

Share to Pseudomonas aeruginosa

Share to Structural Homology, Protein

Source

Identifiers

PMID: 28524228
DOI: 10.1002/1873-3468.12683

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and characterization of a NAD(P)H-dependent carbonyl reductase from Pseudomonas aeruginosa PAO1.PMID 28524228Read ↗

Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.Semantic proximity Read ↗

In Silico Characterization of a Hypothetical Protein from <i>Pseudomonas aeruginosa</i> LESB58: A Structural and Functional PerspectiveSemantic proximity Read ↗

Crystal Structure of a Histone Deacetylase Homologue from Pseudomonas aeruginosaSemantic proximity Read ↗

Structural Comparison of Acinetobacter baumannii β-ketoacyl-acyl Carrier Protein Reductases in Fatty Acid and Aryl Polyene BiosynthesisSemantic proximity Read ↗

The Protein Interaction Networks of Catalytically-Active and Catalytically-Inactive PqsE in <i>Pseudomonas aeruginosa</i>Semantic proximity Read ↗

Dihydrolipoamide dehydrogenase of Pseudomonas aeruginosa is a surface-exposed immune evasion protein that binds three members of the factor H family and plasminogen.Semantic proximity Read ↗

Crystal structure and functional analysis of the extradiol dioxygenase LapB from a long-chain alkylphenol degradation pathway in Pseudomonas.Semantic proximity Read ↗

The role of short-chain dehydrogenase/oxidoreductase, induced by salt stress, on host interaction of B. pseudomalleiSemantic proximity Read ↗

Investigating the reaction and substrate preference of indole-3-acetaldehyde dehydrogenase from the plant pathogen Pseudomonas syringae PtoDC3000.Semantic proximity Read ↗

The PqsE active site as a target for small molecule antimicrobial agents against <i>Pseudomonas aeruginosa</i>Semantic proximity Read ↗

Sent packing: protein engineering generates a new crystal form of Pseudomonas aeruginosa DsbA1 with increased catalytic surface accessibility.Semantic proximity Read ↗

Mutation of a distal gating residue modulates NADH binding in NADH:Quinone oxidoreductase from Pseudomonas aeruginosa PAO1.Semantic proximity Read ↗

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