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Catalysis of a site-specific breakage and reunion reaction that generates two hairpin telomeres from a replicated telomere substrate. Occurs via a two-step transesterification with a protein-DNA intermediate similar to that used by topoisomerases and site-specific recombinases. Catalysis of a ring closure reaction. Catalysis of the ligation of two substances with concomitant breaking of a diphosphate linkage, usually in a nucleoside triphosphate. Ligase is the systematic name for any enzyme of EC class 6. Catalysis of the identification and base-pairing of homologous sequences between single-stranded DNA and double-stranded DNA. Catalysis of the reaction: octanoic acid + 2 S = lipoic acid + 2 H. Catalysis of the activation of small proteins, such as ubiquitin or ubiquitin-like proteins, through the formation of an ATP-dependent high-energy thiolester bond. Catalysis of the reaction: methylglyoxal + H2O = D-lactate. Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. Catalysis of the transposition of transposable elements or transposons. Transposases are involved in site-specific DNA recombination required for transposition in bacteria and other organisms. Catalysis of the second transesterification reaction of spliceosomal mRNA splicing. Ligation of the two exons occurs via a transesterification reaction where the free 3'-hydroxyl group of the 5' exon is the nucleophile attacking the 3' splice site. Non-expressed sequences are now detached from the exons. In cis splicing, the intron is in a lariat structure. Catalysis of the reaction: 7,8-dihydroneopterin triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + PPPi. Elemental activities, such as catalysis or binding, describing the actions of a gene product at the molecular level. A given gene product may exhibit one or more molecular functions. Catalysis of the first transesterification reaction of spliceosomal mRNA splicing. The intron branch site adenosine is the nucleophile attacking the 5' splice site, resulting in cleavage at this position. In cis splicing, this is the step that forms a lariat structure of the intron RNA, while it is still joined to the 3' exon. Catalysis of the formation of new phosphodiester bonds between a pair of short, unique DNA target sequences. null Catalysis of the reaction: iminoaspartate + dihydroxy-acetone-phosphate = quinolinate + 2 H2O + phosphate. Catalysis of the reaction UDP-D-glucose + NADPH = UDP-L-rhamnose + NADP+ + H2O. null null Catalysis of the sulfurylation of the desulfo form of molybdenum cofactor (MoCo), a cofactor required for the activity of some enzymes, such as aldehyde oxidase. null Catalysis of the removal of an amino group from a substrate, producing ammonia (NH3). Catalysis of a reaction that generates a free radical, a highly reactive molecule with an unsatisfied electron valence pair. Catalysis of a reaction in which S-adenosyl-L-methionine (SAM) undergoes reductive cleavage to serve as a source of the 5'-deoxyadenosyl radical. Catalysis of the reaction: prephytoene pyrophosphate = phytoene + pyrophosphate. Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. Catalysis of the integration of lambdoid phage DNA during establishment, probably by forming a transient DNA-protein link. Catalysis of the conversion of precursor Z to molybdopterin, the final step in molybdopterin biosynthesis. Catalysis of the removal of a methyl group from a substrate. Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3. Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. Catalysis of the ring closure reaction: versiconal hemiacetal = versicolorin B + H2O. Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. null Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. Catalysis of the cleavage of branch points in branched glycogen polymers.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: catalytic activity
Acc: GO:0003824
Aspect: Molecular Function
Desc: Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
Synonyms:
  • enzyme activity
Proteins in PDR annotated with:
   This term: 4869 [Search]
   Term or descendants: 52298 [Refine Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0003824 - catalytic activity (interactive image map)

YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle