PXD005934-1

PXD005934 is an original dataset announced via ProteomeXchange.

Title	Enzymatic activation of the nitrogen atom in peptide bonds
Description	Abstract 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.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_10:06:23.535.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD005934
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Sally Shirran
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	Oxidation
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2017-02-20 01:36:54	ID requested
⏵ 1	2024-10-07 10:06:24	announced

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, ü, 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;

curator keyword: Biological

submitter keyword: amide chemistry and biochemistry,Methylation, enzyme catalysis

Sally Lorna Shirran
contact affiliation	Biomedical Sciences Research Complex University of St Andrews
contact email	ss101@st-andrews.ac.uk
lab head
Sally Shirran
contact affiliation	University of St Andrews
contact email	ss101@st-andrews.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD005934
     1. Label: PRIDE project
     2. Name: Enzymatic activation of the nitrogen atom in peptide bonds