Enzymes

specific biologic proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition.

The different forms may be differentiated from each other based on certain physical properties, such as electrophoretic mobility, solubility, or resistance to inactivation.

results when an enzyme is subject to posttranslational modifications.

a nonprotein molecule, called a _____, may be necessary for enzyme activity.

Inorganic cofactors, such as chloride or magnesium ions, are called

is an organic cofactor, such as nicotinamide adenine dinucleotide (NAD).

When bound tightly to the enzyme, the coenzyme is called a

The enzyme portion ______, with its respective coenzyme, forms a complete and active system, a ______.

Catalyze an oxidation–reduction reaction between two substrates

Catalyze the transfer of a group other than hydrogen from one substrate to another

Catalyze hydrolysis of various bonds

Catalyze removal of groups from substrates without hydrolysis; the product contains double bonds

Catalyze the interconversion of geometric, optical, or positional isomers

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bond in adenosine triphosphate (ATP) or a similar compound

The excess energy, called _________, is the energy required to raise all molecules in 1 mole of a compound at a certain temperature to the transition state at the peak of the energy barrier.

refers to enzymes that predominantly combine with only one optical isomer of a certain compound.

the reaction rate is directly proportional to substrate concentration.

the reaction rate depends only on enzyme concentration.

is the substrate concentration at which the reaction velocity is half of the maximum level.

more accurate and convenient determination of Vmax and Km may be made through a ____________, a double-reciprocal plot of the Michaelis-Menten constant,

For each __ degree increase in temperature, the rate of the reaction will approximately double

The rate of denaturation increases as the temperature increases and is usually significant at

physically bind to the active site of an enzyme and compete with the substrate for the active site.

binds an enzyme at a place other than the active site and may be reversible in the respect that some naturally present metabolic substances combine reversibly with certain enzymes.