Inositol-Phosphate Phosphatase
https://en.m.wikipedia.org/wiki/Inositol-phosphate_phosphatase
Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7729029/
Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein
https://www.pnas.org/doi/10.1073/pnas.121190898
Both N-Terminal and C-Terminal Histidine Residues of the Prion Protein Are Essential for Copper Coordination and Neuroprotective Self-Regulation
https://www.sciencedirect.com/science/article/abs/pii/S0022283620303697
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The eighth step of L-histidine biosynthesis is carried out by an enzyme called histidinol-phosphate phosphatase (HolPase). Three unrelated HolPase families are known so far.
Two of them are well studied: HAD-type HolPases known from Gammaproteobacteria like Escherichia coli or Salmonella enterica and PHP-type HolPases known from yeast and Firmicutes like Bacillus subtilis.
However, the third family of HolPases, the inositol monophosphatase (IMPase)-like HolPases, present in Actinobacteria like Corynebacterium glutamicum (HisN) and plants, are poorly characterized.
Moreover, there exist several IMPase-like proteins in bacteria (e.g. CysQ, ImpA, and SuhB) which are very similar to HisN but most likely do not participate in L-histidine biosynthesis.
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https://en.m.wikipedia.org/wiki/Glucuronidation
Various glycoside hydrolases have shown efficacy in degrading matrix polysaccharides within the extracellular polymeric substance (EPS) of microbial biofilms. Medically, biofilms afford infectious microorganisms a variety of advantages over their planktonic, fre-floating counterparts, including greatly increased tolerances to antimicrobial agents and the host immune system. Thus, degrading the biofilm may increase antibiotic efficacy, and potentiate host immune function and healing ability. A combination of alpha-amylase and cellulase was shown to degrade polymicrobial bacterial biofilms from both in vitro and in vivo sources, and increase antibiotic effectiveness against them.
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Heparan Sulfate
Copper
A new convergent chemoenzymatic synthesis strategy, integrating enzymatic synthesis of heparan sulfate, sortase A ligation, copper(i)-catalyzed alkyne-azide cycloaddition, and solid phase peptide synthesis, has been established to efficiently synthesize a mimetic of heparan sulfate proteoglycan syndecan-1 glyco-polypeptide at a milligram scale.
heparan sulfate mimetics having a domain structure were synthesized by copper catalyzed alkyne-azide cycloaddition of HS oligosaccharide having a terminal alkyne or azide moiety.
Heparan sulfate penetrates the membrane and is transported to the nucleus. This process is dependent on copper and on expression and processing of the amyloid precursor protein.
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O-GlcNAc
O-GlcNAcylation
In Alzheimer’s disease, a cytosolic phosphoprotein called Tau, is abnormally phosphorylated. The reason for this was attributed to an overall decrease in O-GlcNAcylation, a novel type of O-glycosylation by which the monosaccharide β-N-acetylglucosamine (GlcNAc) attaches to serine /threonine residues via an O-linked glycosidic bond.
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Asparagine Peptide Lyase
Intein-Containing Proteins
An intein is a protein contained within another protein, the extein. Parasitic DNA infects an intein gene, which encodes an endonuclease. The resulting cDNA (complementary DNA) encodes the extein along with the intein. The intein contains a self-cleaving domain, which has the endonuclease nested within it. The intein domain performs two proteolytic cleavages at its own N-terminus and C-terminus and releases from the extein, separating it in two fragments.
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Protein Splicing
https://en.m.wikipedia.org/wiki/Protein_splicing
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The microtubule-associated protein tau is abnormally hyperphosphorylated when isolated from the brain of patients who suffer from Alzheimer's disease. This is due to the dysfunction of dephosphorylation mechanisms at specific amino acids on the tau protein. Tau dephosphorylation is catalysed by protein phosphatase-2A and phosphatase-2B.
https://en.m.wikipedia.org/wiki/Dephosphorylation
Phosphatase
Phosphorylase Kinase
Glycogen Phosphorylase
Phosphoglycerate Kinase
Hexokinase
https://en.m.wikipedia.org/wiki/Phosphatase
https://en.m.wikipedia.org/wiki/Phosphorylase
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Lipid-protein interactions modulate the conformational equilibrium of a potassium channel
https://www.nature.com/articles/s41467-020-15741-8
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1H, 15N, 13C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5594045/
Phosphoglycerate kinase is a bisubstrate magnesium-dependent enzyme with highly conserved amino acid sequences found in all living organisms.
Magnetic isotope effect of magnesium in phosphoglycerate kinase phosphorylation
https://www.pnas.org/doi/10.1073/pnas.0504876102
Phosphoglycerate kinase (PGK) is found to be controlled by a 25Mg2+-related magnetic isotope effect. Mg2+ nuclear spin selectivity manifests itself in PGK-directed ADP phosphorylation, which has been clearly proven by comparison of ATP synthesis rates estimated in reaction mixtures with different Mg isotopy parameters.
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Myelin
Ranvier
TREK
TRAAK
Lipid
Potassium
Mechanosensitivity is mediated directly by the lipid membrane in TRAAK and TREK1 K+ channels
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