All terms in GO

Label Id Description
obsolete peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan GO_0019800 [OBSOLETE. The formation of a cross-link between peptide chains mediated by a chondroitin 4-sulfate glycosaminoglycan that originates from a typical O-glycosidic link to serine of one chain; the other chain is esterified, via the alpha-carbon of its C-terminal Asp, to C-6 of an internal N-acetylgalactosamine of the glycosaminoglycan chain.]
cyclization of asparagine involved in intein-mediated protein splicing GO_0019801 [The cyclization of asparagine to yield an L-aspartimide (otherwise known as alpha-aminosuccinimide) residue at the C-terminus of an excised intein during protein splicing.]
asparagine metabolic process GO_0006528 [The chemical reactions and pathways involving asparagine, 2-amino-3-carbamoylpropanoic acid.]
cyclization of glutamine involved in intein-mediated protein splicing GO_0019802 [The cyclization of glutamine to yield an L-glutamimide residue at the C-terminus of an excised intein during protein splicing.]
glutamine metabolic process GO_0006541 [The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.]
obsolete peptidyl-aspartic acid carboxylation GO_0019803 [OBSOLETE. The carboxylation of peptidyl-aspartic acid to form peptidyl-L-beta-carboxyaspartic acid.]
obsolete quinolinate synthetase complex GO_0019804 [OBSOLETE. A heterodimer which acts as a quinolinate synthetase; quinolinate synthetase B (L-aspartate oxidase) catalyzes the oxidation of L-aspartate to L-iminoaspartate; quinolinate synthetase A condenses L-imidoaspartate and dihydroxyacetone to quinolinate.]
quinolinate biosynthetic process GO_0019805 [The chemical reactions and pathways resulting in the formation of quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.]
quinolinate metabolic process GO_0046874 [The chemical reactions and pathways involving quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.]
pyridine-containing compound biosynthetic process GO_0072525 [The chemical reactions and pathways resulting in the formation of a pyridine-containing compound, i.e. any compound that contains pyridine or a formal derivative thereof.]
bromide peroxidase activity GO_0019806 [Catalysis of the reaction: 2 R-H + 2 bromide + H2O2 = 2 R-Br + 2 H2O. Enzymes with this activity often accept other halide ions as substrates, including chloride and iodide.]
haloperoxidase activity GO_0140905 [Catalysis of the reaction: R-CH + a halogen + H2O2 = R-C-halogen + H2O.]
GO_0019818 GO_0019818
P1 peroxisome GO_0019819 [A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P1 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they contain fewer peroxisomal proteins than the other subforms.]
peroxisome GO_0005777 [A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.]
putrescine binding GO_0019810 [Binding to putrescine, 1,4-diaminobutane, the polyamine formed by decarboxylation of ornithine and the metabolic precursor of spermidine and spermine.]
cocaine binding GO_0019811 [Binding to cocaine (2-beta-carbomethoxy-3-beta-benzoxytropane), an alkaloid obtained from dried leaves of the South American shrub Erythroxylon coca or by chemical synthesis.]
heterocyclic compound binding GO_1901363 [Binding to heterocyclic compound.]
type I site-specific deoxyribonuclease complex GO_0019812 [A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell.]
endodeoxyribonuclease complex GO_1905347 [A protein complex which is capable of endodeoxyribonuclease activity.]