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During adenylylation, there is a nucleophilic attack on the alpha phosphate of ATP from a catalytic lysine resulting in the production of inorganic pyrophosphate (PPi) and a covalently bound lysine-AMP intermediate in the active site of DNA ligase 1. During the AMP transfer step, the DNA ligase becomes associated with the DNA, locates a nick ...
27401 Ensembl ENSG00000145604 ENSMUSG00000054115 UniProt Q13309 Q9Z0Z3 RefSeq (mRNA) NM_001243120 NM_005983 NM_032637 NM_001285980 NM_013787 NM_145468 RefSeq (protein) NP_001230049 NP_005974 NP_116026 NP_001272909 NP_038815 Location (UCSC) Chr 5: 36.15 – 36.2 Mb Chr 15: 9.11 – 9.16 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse S-phase kinase-associated protein 2 is an enzyme ...
DNA ligase is a type of enzyme that facilitates the joining of DNA strands together by catalyzing the formation of a phosphodiester bond.It plays a role in repairing single-strand breaks in duplex DNA in living organisms, but some forms (such as DNA ligase IV) may specifically repair double-strand breaks (i.e. a break in both complementary strands of DNA).
S phase (Synthesis phase) is the phase of the cell cycle in which DNA is replicated, occurring between G 1 phase and G 2 phase. [1] Since accurate duplication of the genome is critical to successful cell division, the processes that occur during S-phase are tightly regulated and widely conserved.
Skp, Cullin, F-box containing complex (or SCF complex) is a multi-protein E3 ubiquitin ligase complex that catalyzes the ubiquitination of proteins destined for 26S proteasomal degradation. [1] Along with the anaphase-promoting complex, [2] SCF has important roles in the ubiquitination of proteins involved in the cell cycle. The SCF complex ...
In biochemistry, a ligase is an enzyme that can catalyze the joining of two molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds.
The mechanism of the ligation reaction was first elucidated in the laboratory of I. Robert Lehman. [4] [5] Two fragments of DNA may be joined by DNA ligase which catalyzes the formation of a phosphodiester bond between the 3'-hydroxyl group (-OH) at one end of a strand of DNA and the 5'-phosphate group (-PO4) of another.
The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as CUL9 , also known as p53 cytoplasmic anchor PARC , and the ANAPC2 subunit of the anaphase-promoting complex/cyclosome; both CUL9 and ANAPC2 have ubiquitin ligase activity.