Search results
Results from the WOW.Com Content Network
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 ...
A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement ...
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.
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).
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.
At the start of the ubiquitination cascade, the E1 enzyme (Figure 2) binds ATP-Mg 2+ and ubiquitin and catalyses ubiquitin C-terminal acyl adenylation. [4] In the next step a catalytic cysteine (Figure 3) on the E1 enzyme attacks the ubiquitin-AMP complex through acyl substitution, simultaneously creating a thioester bond and an AMP leaving group. [2]
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 ...