Usually there are three kinds of proteins that could bind to an enzyme to enhance its catalytic activity. The prosthetic groups are one that are firmly attched to the enzymes. The best example of a prosthetic group is heme that is bound to hemoglobin.
The next is co factor, that could dissociate itself from the enzyme, like NADH and NADPH.
Cofactor, finally, are metal ions, usually cations, that bind to the metal ions and enhance the activity. they perform certain functions; as to hold the substrates in close proximity. The best example is DNA and RNA polymerase, where the upcoming nucleotide is held in the catalytic cleft of polymerase by Magnesium ions.
.its trypsin
Yes, Mg2+ is a cofactor for the enzymes phosphofructo kinase-1, phosphoglycerate kinase, enolase, and pyruvate kinase in glycolysis.
cofactor
tetrahydrofolate (THF)
One of two or more contributing factors.
Cofactor Genomics was created in 2008.
the general term is cofactor, but more specifically, if the cofactor is an organic molecule, it is called a coenzyme
No .
.its trypsin
Mg2+ is a cofactor of the enzyme peroxidase. In order to keep the enzyme active, this cofactor must be supplied. Magnesium chloride dissociates in solution into magnesium and chloride ions. The cofactor requirement is thus met
It is not possible to determine whether an enzyme requires a cofactor from these data.
Yes, Mg2+ is a cofactor for the enzymes phosphofructo kinase-1, phosphoglycerate kinase, enolase, and pyruvate kinase in glycolysis.
CO-ENZYME: A dissociable cofactor, usually organic. PROSTHETIC GROUP: non-dissociable cofactor.
calcium
Magnesium
enzyme cofactor
It is known as the cofactor.