Blatant Biology

catalytic mechanism allowing the lowering of activation energy by an enzyme, by using an alternative reaction pathway forming a covalent intermediate; catalyst must be a better nucleophile than water (or whatever the original nucleophile is)

enzyme class cleaving peptide bonds in proteins, found in both eukaryotes and prokaryotes; 2 types: chymotrypsin-like and subtilisin-like

substitution reaaction by an electron-rich species replacing a functional group on an electron-deficient molecule

numerical classification system for enzymes, based on the reactions they catalyse

class of enzyme catalysing proteolysis, hydrolysing peptide bonds

the covalent bond broken by an enzyme

chemical reaction breaking a molecule down through the use of water

class of hydrolase enzymes degrading proteins, with a conserved catalytic dyad/triad, with a common thiol group

protease enzyme with a catalytic mechanism involving a metal ion

class of serine proteases found in the small intestine, hydrolysing proteins, typically at the carbonyl side of lysine or aginine residues

enzyme with a metal ion cofactor required for catalytic activity

an inactive form of an enzyme, which must undergo conversion to become the active, catalytic form

an inactive substance that is metabolised into an enzyme

a serine protease inhibitor, frequently used while preparing cell lysates

protease inhibitor used while preparing protein and cell isolates

protease inhibitor, irreversibly inhibiting chymotrypsin and some cysteine proteases, but not trypsin or zymogens

an area in an enzyme active site, stabilising intermediate negative charges on deprotonated oxygens or alkoxides, loweing the activation energy required for the reaction