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PXD005934-1

PXD005934 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleEnzymatic activation of the nitrogen atom in peptide bonds
DescriptionAbstract The peptide bond is the defining feature of proteins, it co ntrols their structure by enforcing planarity and governs their chemistry by abolishing nucleophili city. This behaviour results from the delocalisation of the lone pair of electrons on the nitrogen atom into the adjacent carbonyl bond. Methylating an amide bond by conventional chemistry usually requires a metal to generate the amide anion. The OphA enzyme methyla tes amide bonds at pH 7 in water using S-adenosyl methionine (SAM) as co-factor. The st ructure of OphA reveals a complex catenane arrangement in which the substrate i s clamped adjacent to SAM. Site directed mutants have identified the key catalytic residue s. A mechanism in which conjugation of the peptide bond is disrupted by van der Waals in teractions between SAM and the amide nitrogen is proposed and tested. The methylation of amides is of particular interest as it greatly enhances the cell permeability of peptides.
HostingRepositoryPRIDE
AnnounceDate2024-10-07
AnnouncementXMLSubmission_2024-10-07_10:06:23.535.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD005934
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterSally Shirran
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListOxidation
InstrumentTripleTOF 5600
Dataset History
RevisionDatetimeStatusChangeLog Entry
02017-02-20 01:36:54ID requested
12024-10-07 10:06:24announced
Publication List
Song H, van der Velden NS, Shiran SL, Bleiziffer P, Zach C, Sieber R, Imani AS, Krausbeck F, Aebi M, Freeman MF, Riniker S, K, ΓΌ, nzler M, Naismith JH, A molecular mechanism for the enzymatic methylation of nitrogen atoms within peptide bonds. Sci Adv, 4(8):eaat2720(2018) [pubmed]
10.1126/sciadv.aat2720;
10.6019/PXD005934;
Keyword List
curator keyword: Biological
submitter keyword: amide chemistry and biochemistry,Methylation, enzyme catalysis
Contact List
Sally Lorna Shirran
contact affiliationBiomedical Sciences Research Complex University of St Andrews
contact emailss101@st-andrews.ac.uk
lab head
Sally Shirran
contact affiliationUniversity of St Andrews
contact emailss101@st-andrews.ac.uk
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
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