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ProteomicsQuantitative chemoproteomic identification of lysine carboxylation in proteins
Carbon dioxide is an abundant biological gas that drives adaptive physiological responses within organisms from all domains. The basic biochemical mechanisms by which proteins serve as sensors of CO2 are, therefore, of great interest. CO2 is a potent electrophilic, and thus one way it can modulate p...
ORGANISM(S): Escherichia coli Synechocystis sp. 
2023-09-09 | PXD031976 | Pride
Co2 Lysine carboxylation Chemoproteomics Homocitrulline 
ProteomicsStructural mechanism of γ-carboxylation coupled to vitamin K epoxidation at membrane interface
Hemostasis and various non-hemostatic physiologies require γ-carboxylation of designated glutamates in vitamin K-dependent proteins (VKDPs), a process coupled with epoxidation of vitamin K hydroquinone (KH2) by membrane-integrated γ-carboxylase (VKGC). To understand this unique biochemistry, we dete...
ORGANISM(S): Homo sapiens (Human) 
2025-12-22 | PXD052939 | Pride
Factor ix Vitamin k epoxide Vkgc Fix Γ-carboxylation Tmg2 
ProteomicsMolecular basis of vitamin K driven γ-carboxylation at membrane interface
The γ-carboxylation of glutamate residues enables Ca2+-mediated membrane assembly of protein complexes that support broad physiological functions including hemostasis, calcium homeostasis, immune response, and endocrine regulation. Modulating γ-carboxylation level provides prevalent treatments for h...
ORGANISM(S): Homo sapiens (Human) 
2026-01-26 | PXD059315 | Pride
Human Electron microscopy Cryo-em Post-translational modifications Lc-ms/ms 
UnknownLysine carboxylation: unveiling a spontaneous post-translational modification.
Not available
S-EPMC3919261 | biostudies-literature
ProteomicsSystematic analysis of lysine malonylation in Streptococcus mutans
Lysine malonylation is an evolutionarily conserved PTM from bacteria to mammals and involves malonyl-coenzyme (CoA) as a cofactor. Since the malonyl group has an acidic carboxylic group under physiological pH, malonylated lysine is negatively charged, which might impact on protein function and enzym...
ORGANISM(S): Streptococcus mutans UA159 
2022-11-17 | PXD038045 | Pride
Malonylation Biofilm Post-translational modification Streptococcus mutans 
UnknownIn-depth profiling of lysine-producing Corynebacterium glutamicum by combined analysis of the transcriptome, metabolome, and fluxome.
Not available
S-EPMC355958 | biostudies-literature
UnknownLysine Nzeta-decarboxylation switch and activation of the beta-lactam sensor domain of BlaR1 protein of methicillin-resistant Staphylococcus aureus.
Not available
S-EPMC3173090 | biostudies-literature
UnknownReversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.
Not available
S-EPMC2959125 | biostudies-literature
MetabolomicsMitochondrial glutamine import sustains mitochondrial translation independent of glutaminolysis in cancer_GlnFlux_untargeted metabolites

Oxidative phosphorylation (OXPHOS) fulfills energy metabolism and biosynthesis through tricarboxylic acid (TCA) cycle and an intact electron transport chain (ETC). Mitochondrial glutamine import (MGI) replenishes TCA cycle through glutaminolysis, but its broader roles in cancer remains unclear. H...

2025-09-29 | MTBLS13074 | MetaboLights
MetabolomicsMitochondrial glutamine import sustains mitochondrial translation independent of glutaminolysis in cancer_targeted metabolites

Oxidative phosphorylation (OXPHOS) fulfills energy metabolism and biosynthesis through tricarboxylic acid (TCA) cycle and an intact electron transport chain (ETC). Mitochondrial glutamine import (MGI) replenishes TCA cycle through glutaminolysis, but its broader roles in cancer remains unclear. H...

2025-09-29 | MTBLS13076 | MetaboLights
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