Proteomics

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Intact protein mass analysis of wild-type and mutants of glutamine amidotransferase from Methanocaldococcus jannaschii

ABSTRACT: The glutamine amidotransferase (GATase) from Methanocaldococcus jannaschii (Mj) harbours a stable post-translational modification, succinimide (SNN). As shown from earlier studies, the spontaneous deamidation of Asn109 leading to the formation of stable SNN in MjGATase, imparts hyper-thermostability to the protein. To examine which of the residues in the environment of Asn109 catalyses the conversion of Asn to SNN, several mutants of MjGATase were generated. The intact protein masses of these mutants along with the wild-type enzyme were obtained through mass spectrometric analysis. The wild-type enzyme shows a mass difference of 17 Da due to the formation of SNN whereas, the MjGATase mutants harboring unmodified Asn109 would retain the mass corresponding to that obtained from the sequence. The mass analysis of 12 MjGATase mutant proteins showed varied levels retaining intact Asn109 residue. Two double mutants showed almost entire population with the expected mass, thus, highlighting the involvement of the neighbouring residues in formation of SNN.

INSTRUMENT(S):

ORGANISM(S): Methanocaldococcus Jannaschii

SUBMITTER: Hemalatha Balaram  

LAB HEAD: Hemalatha Balaram

PROVIDER: PXD075095 | Pride | 2026-06-08

REPOSITORIES: pride

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Dataset's files

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Action DRS
MjGATase_D110N_1.raw Raw
MjGATase_D110N_240822run_10cutoff.xlsx Xlsx
MjGATase_D110P_1.raw Raw
MjGATase_D110P_15.xlsx Xlsx
MjGATase_D110V_1.raw Raw
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Publications

Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase.

Chandrashekarmath Anusha A   Jash Oishika O   Singh Karandeep K   Bellur Asutosh A   Roy Chitralekha Sen CS   Dongre Aparna A   Chathoth Nayana Edavan NE   Anjukandi Padmesh P   Kumar Sanjeev S   Mukherjee Souradip S   Balaram Padmanabhan P   Balasubramanian Sundaram S   Balaram Hemalatha H  

The Journal of biological chemistry 20260428 6

Succinimide (SNN), an intermediate spontaneously formed during asparaginyl deamidation or aspartyl dehydration in proteins, is generally hydrolysis-prone, leading to isomerization to an L/D α/β-aspartyl residue, with the latter being considered deleterious to protein structure and function. An unusually stable SNN-mediated conformational rigidity through restriction of the backbone dihedral angle, ψ, enhances the thermostability of glutamine amidotransferase (GATase) from Methanocaldococcus jann  ...[more]

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