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, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI.

The Journal of biological chemistry - 21 Apr 2006

Song Feng, Zhuang Zhihao, Finci Lorenzo, Dunaway-Mariano Debra, Kniewel Ryan, Buglino John A, Solorzano Veronica, Wu Jin, Lima Christopher D

Abstract excerpt

The structure and biochemical function of the hot dog-fold thioesterase PaaI operative in the aerobic phenylacetate degradation pathway are examined. PaaI showed modest activity with phenylacetyl-coenzyme A, suggestive of a role in coenzyme A release from this pathway intermediate in the event of limiting downstream pathway enzymes. Minimal activity was observed with aliphatic acyl-coenzyme A thioesters, which...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Hydrogen-Ion Concentration

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

Share to Hydrolysis

Share to Models, Chemical

Share to Phenylacetates

Share to Protein Folding

Share to Protein Structure, Quaternary

Share to Static Electricity

Source

Identifiers

PMID: 16464851
DOI: 10.1074/jbc.M513896200

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

Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI.PMID 16464851Read ↗

The role of lysine(100) in the binding of acetylcoenzyme A to human arylamine N-acetyltransferase 1: implications for other acetyltransferases.Semantic proximity Read ↗

A Single-Site Mutation at Ser146 Expands the Reactivity of the Oxygenase Component of p-Hydroxyphenylacetate 3-Hydroxylase.Semantic proximity Read ↗

Significant catalytic roles for Glu47 and Gln 110 in all four of the C-C bond-making and -breaking steps of the reactions of acetohydroxyacid synthase II.Semantic proximity Read ↗

Specificity determinants for the pyruvate dehydrogenase component reaction mapped with mutated and prosthetic group modified lipoyl domains.Semantic proximity Read ↗

The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition.Semantic proximity Read ↗

Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.Semantic proximity Read ↗

Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli.Semantic proximity Read ↗

Involvement of the Pta-AckA pathway in protein folding and aggregation.Semantic proximity Read ↗

Naturally impaired side-chain shortening of aromatic 3-ketoacyl-CoAs reveals the biosynthetic pathway of plant acetophenones.Semantic proximity Read ↗

Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study.Semantic proximity Read ↗

A nucleophilic catalysis step is involved in the hydrolysis of aryl phosphate monoesters by human CT acylphosphatase.Semantic proximity Read ↗

The catalytic mechanism of the hotdog-fold enzyme superfamily 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU.Semantic proximity Read ↗

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