All terms in GO
Label | Id | Description |
---|---|---|
asparagine metabolic process | GO_0006528 |
The chemical reactions and pathways involving asparagine, 2-amino-3-carbamoylpropanoic acid.
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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.
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glutamine metabolic process | GO_0006541 |
The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
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peptidyl-aspartic acid carboxylation | GO_0019803 |
The carboxylation of peptidyl-aspartic acid to form peptidyl-L-beta-carboxyaspartic acid.
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protein carboxylation | GO_0018214 |
The addition of a carboxy group to a protein amino acid.
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peptidyl-aspartic acid modification | GO_0018197 |
The modification of peptidyl-aspartic acid.
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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.
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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.
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quinolinate metabolic process | GO_0046874 |
The chemical reactions and pathways involving quinolinate, the anion of quinolinic acid, also known as 2,3-pyridinedicarboxylic acid.
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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.
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bromide peroxidase activity | GO_0019806 |
Catalysis of the reaction: 2 R-H + 2 bromide + hydrogen peroxide = 2 R-Br + 2 H2O. Enzymes with this activity often accept other halide ions as substrates, including chloride and iodide.
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peroxidase activity | GO_0004601 |
Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O.
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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.
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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.
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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.
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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.
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heterocyclic compound binding | GO_1901363 |
Binding to heterocyclic compound.
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organic cyclic compound binding | GO_0097159 |
Binding to an organic cyclic compound, any molecular entity that contains carbon arranged in a cyclic molecular structure.
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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.
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