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The incorporation of sarcosine (N-methylglycine) into non-coded peptides. The formation of the non-fluorescent protein chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamic acid, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like non-fluorescent red chromoprotein from the sea anemone Radianthus macrodactylus. The methylation of the N-terminal glycine of proteins to form the derivative N-methylglycine. The formation of the fluorescent protein FP611 chromophore cross-link from the alpha-carboxyl carbon of residue n, a methionine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. This modification is found in the GFP-like fluorescent chromoprotein from the sea anemone Entacmaea quadricolor. The modification of peptidyl-glycine. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl glycine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl glycine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The chemical reactions and pathways resulting in the formation of peptidyl-1-thioglycine from other compounds, including peptidyl-glycine. The acetylation of the N-terminal glycine of proteins to form the derivative N-acetylglycine. The alteration of an amino acid residue in a peptide. The formation of a protein active site cross-link from the alpha-carboxyl carbon of residue n, an alanine, serine or cysteine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with an oxidation of residue n+1 to form an active aldehyde. The formation of an isopeptide cross-link between peptidyl-glutamate and peptidyl-glycine to produce N-(L-isoglutamyl)-glycine, as found in the antibiotic microcin J25. The formation of S-(peptidyl-glycyl)-peptidyl-cysteine cross-links by the formation of a thiolester between cysteine and the carboxy-terminal glycine of ubiquitin and other proteins. The formation of an isopeptide cross-link between peptidyl-lysine and peptidyl-glycine to produce N6-glycyl-L-lysine. This is distinct from the formation of the thiolester intermediate, which occurs during ubiquitination. The formation of the fluorescent protein FP583 chromophore cross-link from the alpha-carboxyl carbon of residue n, a glutamine, to the alpha-amino nitrogen of residue n+2, a glycine, and a dehydration to form a double bond to the alpha-amino nitrogen of residue n+1. This cross-linking is coupled with a dehydrogenation of residue n+1 to form a double bond between the alpha and beta carbons. The glucuronylation of the N-terminal glycine of proteins to form the derivative D-glucuronyl-N-glycine. The myristoylation of the N-terminal glycine of proteins to form the derivative N-myristoyl-glycine. The formylation of the N-terminal glycine of proteins to form the derivative N-formylglycine. The formation of a C-terminal peptidyl-glycine acid amide by hydrolysis and oxidation of an interior Gly-Gly peptide in a secreted protein. The formation of an isopeptide cross-link between peptidyl-asparagine and peptidyl-glycine to produce N-(L-isoaspartyl)-glycine. The synthesis of peptidyl-glycine cholest-5-en-3-beta-ol ester at the carboxy-terminus of autolytically cleaved proteins. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-glycine ethanolamide-linked glycosylsphingolipidinositol (GSI) anchor following hydrolysis of a glycyl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-glycine ethanolamide-linked phosphatide following hydrolysis of a glycyl-peptide bond, as in the cleavage of arginine from the carboxy-terminal of Apg8 followed by its amidation with phosphatidylethanolamine. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-glycine ethanolamide-linked glycosylphosphatidylinositol (GPI) anchor following hydrolysis of a glycyl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-glycine modification
Acc: GO:0018201
Aspect: Biological Process
Desc: The modification of peptidyl-glycine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 2 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018201 - peptidyl-glycine modification (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle