ligase

And then we add a ligase, which will glue the two ends back together.

It has been classified both as a ligase and a lyase.

Given set one, the ligase will incorporate any fragments that match perfectly.

In mammals, there are four specific types of ligase.

But, as we noted above, the ligase is fussy about where the phosphates are.

The family of proteins is known to possess ubiquitin-protein ligase activity.

Ligase can only repair the break on the left, where the phosphate group is attached to what's called the 5' carbon.

The systematic name of this enzyme class is 2,3-dihydroxybenzoate:L-serine ligase.

These ends are called cohesive since they are easily joined back together by a ligase.

This gene is a member of the DNA ligase family.

DNA ligase would most likely have to be incorporated and utilized in such a machine.

DNA Ligase then acts to join the two ends together.

The first DNA ligase was purified and characterized in 1967.

It could be an E3 ubiquitin-protein ligase.

In order to ligate these fragments together, the ligase progresses through three steps:

A20, a deubiquitine ligase, has been shown to be cut by paracaspase in Human and in mouse.

In general, a ligase catalyzes the following reaction:

Most obviously, for example, formate-tetrahydrofolate ligase synthesizes 10-formyltetrahydrofolate.

The gene structure is completed by a cellular ligase present in both eukaryotic and prokaryotic cells.

E6-AP is involved in the ubiquitin ligase pathway.

ATP is required for the ligase reaction, which proceeds in three steps:

An E3 ubiquitin ligase targets specific protein substrates for degradation by the proteasome.

Since the overhangs have to be complementary in order for the ligase to work, the two molecules can only join in one orientation.

DNA ligase is then added to join the dye-labelled probe to the primer.

Each E3 ubiquitin ligase binds to a particular set of substrates, causing their ubiquitination.