ArticleThe Journal of biological chemistry2008
Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87).
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Compound Z247611722 Exhibits Antifungal Activity by Inhibiting Serine Palmitoyltransferase.Nature communications · 2026Article
- Adaptive Evolution of the Greater Horseshoe BatAnimals : an open access journal from MDPI · 2024Article
- Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.Nature communications · 2022Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
- Structural Determinants of Substrate Recognition and Catalysis by Heparan Sulfate Sulfotransferases.ACS catalysis · 2021Article
- Insect ArylalkylamineFrontiers in molecular biosciences · 2018Review
- Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine.Scientific reports · 2017Article
- Probing the chemical mechanism and critical regulatory amino acid residues of Drosophila melanogaster arylalkylamine N-acyltransferase like 2.Insect biochemistry and molecular biology · 2015Article
- Article
- Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.Biochemistry · 2014Article
- Drastic neofunctionalization associated with evolution of the timezyme AANAT 500 Mya.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dissecting the metal selectivity of MerR monovalent metal ion sensors in Salmonella.Journal of bacteriology · 2013Article
- Role of the actin Ala-108-Pro-112 loop in actin polymerization and ATPase activities.The Journal of biological chemistry · 2012Article
- Molecular evolution of multiple arylalkylamine N-acetyltransferase (AANAT) in fish.Marine drugs · 2011Article
- Article
- Evolution of AANAT: expansion of the gene family in the cephalochordate amphioxus.BMC evolutionary biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Arylalkylamine N-acetyltransferase (AANAT) catalyzes the N-acetylation of serotonin, the penultimate step in the synthesis of melatonin. Pineal AANAT activity increases at night in all vertebrates, resulting in increased melatonin production. This increases circulating levels of melatonin, thereby providing a hormonal signal of darkness. Kinetic and structural analysis of AANAT has determined that one element is floppy. This element, termed Loop 1, is one of three loops that comprise the arylalkylamine binding pocket. During the course of chordate evolution, Loop 1 acquired the tripeptide CPL, and the enzyme became highly active. Here we focused on the functional importance of the CPL tripeptide and found that activity was markedly reduced when it was absent. Moreover, increasing the local flexibility of this tripeptide region by P64G and P64A mutations had the counterintuitive effect of reducing activity and reducing the overall movement of Loop 1, as estimated from Langevin dynamics simulations. Binding studies indicate that these mutations increased the off-rate constant of a model substrate without altering the dissociation constant. The structural kink and local rigidity imposed by Pro-64 may enhance activity by favoring configurations of Loop 1 that facilitate catalysis and do not become immobilized by intramolecular interactions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.