| Amino Acid Side Chain Properties* | ||
| name | 3 letter | 1 letter |
follow these links for a detailed description |
hover over these links for a molecular structure | |
| Nonpolar | ||
| Alanine | ALA | A |
| Glycine | GLY | G |
| Isoleucine | ILE | I |
| Leucine | LEU | L |
| Methionine | MET | M |
| Proline | PRO | P |
| Valine | VAL | V |
| Aromatic | ||
| Phenylalanine | PHE | F |
| Tryptophan | TRP | W |
| Tyrosine | TYR | Y |
| Polar (Uncharged) | ||
| Serine | SER | S |
| Asparagine | ASN | N |
| Glutamine | GLN | Q |
| Threonine | THR | T |
| Basic 1(uncharged or + charge) | ||
| Lysine | LYS | K |
| Histidine | HIS | H |
| Arginine | ARG | R |
| Acidic 2 (uncharged or - charge) | ||
| Aspartate | ASP | D |
| Glutamate | GLU | E |
| Cysteine3 | CYS | C |
* When addressing the properties of amino acids, one generally means the properties of the side chain only. This is because the the "common" portion is always the same AND is generally involved in peptide bonds.
1 These side chains are uncharged (or neutral) when unprotonated. When protonated then they are postively charged (+1).
2 These side chains are uncharged (or neutral) when protonated. When UNprotonated then they are negatively charged (-1)
3 Cysteine side chain does not end in an organic acid like ASP and GLU, above - but the -SH group does have these same properties of charge. Some texts list this as a polar AA others as acidic - I can go either way.
| Cofactors/Cosubstrates Structures and Chemistries | |||
| Cofactor | ABBR. | Chemistry | Vitamin |
follow these links for a detailed description |
hover over these links for a molecular structure | ||
| Always bound to Enzyme4 | water soluble5 | ||
| B Vitamins | |||
| Thiamine pyrophospate | TPP | Adol reaction α to organic acid | B1 |
| Flavin Adenine dinucleotide | FAD | electron transfer (1 or 2)/ oxidation | B2 |
| Nicotinamide adenine dinucleotide | NAD+ | electron transfer (always 2 as a H-) | B3 |
| Coenzyme A | CoA | acetyl carrier/activator | B5 |
| pyrodoxal phosphate | PLP | amine transfer | B6 |
| biotin | biotin | Addition of carboxyl group via aldol reaction | B7 |
| tetrahydrofolate | THF | methyl/formyl transfer | B9 |
| colbalamin | COBL | unusual radical chemistries | B12 |
| Other Vitamins | |||
| Retinol | VitA | maintenance of the immune system and good vision | A |
| ascorbate | ASC | ROS capture | C |
| cholecalciferol | vitD | absorption of calcium and phosphate | D |
| α-tocopherol | vitE | counteracts the production of ROS in fat | E |
| Phylloquinone | VitK | Essential in the blood clotting cascade | K |
| Non Vitamin derived | |||
| adenosine triphosphate | ATP | phosphate transfer - energy carrier | |
| creatin | cre | phosphate transfer -supplemental energy carrier | |
| protophophyrin IX | heme | electron transfer - oxidations | |
| chlorophyll | chl | light induced electron transfer | |
| Coenzyme Q | CoQ | electron transfer either 1 or 2 | |
| iron-sulfur cluster | FE/S | electron transfer (only 1) elimination | |
| lipoic acid | LipA | acyl transfer for oxidative decarboxylation | |
| S-asenosyl methionine | SAM | methyl transfer | |
4Cofactors that have this background color are always bound to an enzyme and not allowed to diffuse randomly. If the background color is white, then the cofactor is free to diffuse normally and binds to an enzymes active site only during reactions. 5Cofactors that have tyhi sgold background color under the chemsitry are water soluble; if white then soluble in lipids or fats | |||
