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Enzymes turn ATP (adenosine tri-phosphate) into ADP (adenosine di-phosphate) by hydrolyzing off a phosphate group. The removal of that 3rd phosphate group releases a large amount of energy and allows for the enzyme to do a job that would normally be energetically unfavorable.

2007-11-04 04:10:50 · answer #1 · answered by Lisa 3 · 0 0

Various enzymes transfer a P from ATP (converting it into ADP) over to the protein. The energy of ATP is held in it's phosphates (and the most energy is held in that third P) so transferring the P confers energy to the protein.

For example, when muscle contracts, myosin heads bind to actin filaments and pull by bending at the tail and losing a phosphate (energy). Once the myosin has pulled as far as it can, it requires a P from ATP in order to reset to its original position. Without ATP, it can't reset, and the filament becomes 'stuck' (this is what causes rigor mortis). Actin subunits in the cytoskeleton of a cell are also activated by phosphorylation, as well as many signalling molecules (the MAPK cascade, for example, where the enzymes involved are activated by phosphorylation, and then go on to phosphorylate other targets).

Sometimes the binding occurs only in an intermediate step, where a P binds, then quickly unbinds. There is still a transfer of energy, though.

There are several assays that can assess the activity of an enzyme or protein by detecting its phosphorylation state. For example, you could immunostain a cell with an antibody specific for the phosphorylated form of a protein, which could, in turn, tell you whether or not the target protein is active.

2007-11-04 06:05:21 · answer #2 · answered by andymanec 7 · 0 0

quite a few enzymes pass a P from ATP (changing it into ADP) over to the protein. The capability of ATP is held in that's phosphates (and the main capability is held in that 0.33 P) so shifting the P confers capability to the protein. as an occasion, whilst muscle contracts, myosin heads bind to actin filaments and pull by bending on the tail and dropping a phosphate (capability). as quickly as the myosin has pulled so some distance because it may, it demands a P from ATP as a fashion to reset to its unique place. without ATP, it won't be able to reset, and the filament will become 'caught' (that's what reasons rigor mortis). Actin subunits interior the cytoskeleton of a cellular are additionally activated by phosphorylation, as nicely as many signalling molecules (the MAPK cascade, as an occasion, the place the enzymes in touch are activated by phosphorylation, and then go directly to phosphorylate different objectives). sometimes the binding happens purely in an intermediate step, the place a P binds, then at as quickly as unbinds. there continues to be a pass of capability, although. There are quite a few assays that could look into the interest of an enzyme or protein by detecting its phosphorylation state. as an occasion, you could desire to immunostain a cellular with an antibody particular for the phosphorylated form of a protein, that could, in turn, inform you no rely if or no longer the objective protein is lively.

2016-12-15 16:16:48 · answer #3 · answered by Anonymous · 0 0

Energy from ATP is stored in the chemical bonds of the compound

2007-11-04 04:03:49 · answer #4 · answered by Tyler V 2 · 0 0

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