Things to Memorize! Flashcards
Oxidoreductases
Use NADH, NADPH, FADH2
Dehydrogenase, Oxygenase, Oxidase, Hydroxylase, Peroxidase, Reductase, Cytochrome p450
Transferases
transfer groups from one chemical to another;
aminotransferase, kinase, synthase
Hydrolase
Break C-X bond via H20 and results in X-OH
Protease, urease, phosphatase, esterase, peptidase
Lyase
Breaks bond using mechanisms other than hydrolase and oxidoreductase;
decarboxylase and aldolase are examples;
synthases form C=C bonds by removing H20 from COH-CH
Isomerase
rearrangement; mutase, racemase, epimerase
ligase
break a bond using ATP molecule; synthetase
serine protease
in hydrolase class; requires a asp ser his residue; inhibited by serpin, common ones are trypsin, chymotrypsin, elastase, thombin, enteropeptidase;
cysteine protease
cystein residue required; papain, calpain and interleukin-1-b converting enzyme
aspartic proteases
require aspartic acid residue; pepsin, rennin and HIV protease which are all active at low pH due to aspartic acid having a negative R group
metalloprotease
active metal ion required (Zn2+, Co2+, Ca2+); carboxypeptidase, thermolysin, collagenase, mmp
inhibited by EDTA
Thiamine
Vitamin B1 Thiamine pyrophosphate (reacts with aldehydes/ketones to catalyze decarboxylation- cleavage of C-C bond)
Riboflavin
B2
FMN, FADH2
Electrons for redox
Pyridoxine
B6
Pyridoxal Phosphate
reacts with Amines to catalyze amino acid metabolism and transamination reactions
Niacin
NAD, NADP;
shuttles electrons for redox; helps produce ATP
Pantothenic ACid
CoA;
Carries acyl groups (O=C-R) and coenzyme A
Biotin
Covalently attached to carboxylases;
imidazole derivative, attaches to lysine residue of the protein;