We have been cealld the game gurus' amongst our friends (I put them in alphabetic order):- Apples to Apples- Backgammon- Balderdash- Blokus- Cribbage- Demon (cards)- Guesstures- Mille Bourne- Pictionary- RummiKub- Scattegories- Scrabble- Sequence- Settlers of Catan- Skip-bo- Stock Market- Taboo- UpwordsCan you tell we love games ha!!
To convert inactive prothrombin to active thrombin, it is necessary to cleave prothrombin through the action of the enzyme prothrombinase. This complex, primarily composed of factor Xa and factor Va, operates in the presence of calcium ions and phospholipids. The cleavage results in the formation of active thrombin, which plays a crucial role in the coagulation cascade by converting fibrinogen to fibrin and activating additional coagulation factors.
The inactive form of pepsin is called pepsinogen.
Its molecular shape is altered so the substrate cannot fit to its active site
A region on an enzyme that binds to a protein or other substance during a reaction
the substance that an enzyme acts upon is subtrate
A nonprotein compound that combines with an inactive enzyme to form an active enzyme system.
A nonprotein compound that combines with an inactive enzyme to form an active enzyme system.
enzymes are proteins zymogen
To convert inactive prothrombin to active thrombin, it is necessary to cleave prothrombin through the action of the enzyme prothrombinase. This complex, primarily composed of factor Xa and factor Va, operates in the presence of calcium ions and phospholipids. The cleavage results in the formation of active thrombin, which plays a crucial role in the coagulation cascade by converting fibrinogen to fibrin and activating additional coagulation factors.
true
The inactive form of pepsin is called pepsinogen.
The inactive form of a protein splitting enzyme in the stomach is called pepsinogen. It gets converted to its active form, pepsin, when exposed to the acidic environment of the stomach.
Changing the pH in the environment that an enzyme works in can change how active it will be. Most will be active in a narrow range. Pepsin, a stomach enzyme, will only work at very acid pHs and will become inactive at higher pH than 2.
Its molecular shape is altered so the substrate cannot fit to its active site
Apoenzyme is the protein portion of an enzyme, which is inactive without its cofactor or coenzyme. The binding of the cofactor or coenzyme to the apoenzyme forms the active enzyme, allowing it to catalyze a specific biochemical reaction.
A noncompetitive inhibitor is a substance that can bind to the enzyme at a location other than the active site, altering the enzyme's shape and reducing its activity. This type of inhibition does not compete with the substrate for binding to the enzyme.
A region on an enzyme that binds to a protein or other substance during a reaction