Biochemistry — The Amino Acid Encyclopedia

🧬 All Amino Acids

Every amino acid the boards care about, organized by family. Tap any card to flip it and see the clinical details, enzyme associations, and board traps.

The Special One
Gly
Glycine
Simplest Amino Acid
ClaimSmallest amino acid — seen everywhere in the body
UniqueNO chiral carbon — the only amino acid without one (R group = just H)
FunctionInhibitory neurotransmitter for the spinal cord
Board HitTetanus toxin (found in dirt) blocks glycine release from spinal cord → muscles can't relax → diaphragm locks up → can't breathe
💎 Aromatic Amino Acids Big, bulky ring structures
Phe
Phenylalanine
Aromatic • Essential
EnzymeRecognized by chymotrypsin (cuts to its right side)
EnergyBoth glucogenic AND ketogenic
DiseasePKU — can't convert Phe → Tyr → musty/mousy odor, intellectual disability
Trp
Tryptophan
Aromatic • Essential
MakesSerotonin (a monoamine neurotransmitter) and melatonin
AlsoWithout Trp → can't make niacin (B3)Pellagra (3 D's: Dermatitis, Diarrhea, Dementia)
DepletedCarcinoid syndrome uses up all the Trp to make serotonin → Trp deficiency → pellagra
DiseaseHartnup's Disease — Trp spills into the urine (defective neutral AA transporter)
EnergyBoth glucogenic AND ketogenic
Tyr
Tyrosine
Aromatic • Hydroxyl
MakesCatecholamines: Dopamine, Epinephrine, Norepinephrine
AlsoMakes melanin (skin pigment) and thyroid hormones
BondsHas extra OH group → involved in O-linked bonds (phosphorylation target!)
Basic Amino Acids Extra NH₃⁺ = positive charge
Lys
Lysine
Basic • Essential
ChargePositive — extra NH₃⁺ group
EnzymeRecognized by trypsin (cuts to its right side)
EnergyPurely KETOGENIC — one of only 2 (Lys + Leu) 🔑Only KETOGENIC: Lys + Leu. "You can't LIE about KETOgenic — it's only Lysine and LEUcine."
MigratePositive → migrates toward cathode (−)
Arg
Arginine
Basic • Essential
ChargePositive — extra NH₃⁺ group (guanidinium)
EnzymeAlso recognized by trypsin
FunctionPrecursor to nitric oxide (NO) via nitric oxide synthase — vasodilation
MigratePositive → migrates toward cathode (−)
Acidic Amino Acids Extra COO⁻ = negative charge
Asp
Aspartate
Acidic
ChargeNegative — extra COO⁻ group
FunctionReinforcement of behavior via the NMDA pathway (ex: gambling, addictions)
DrugMemantine (and Galantine) blocks glutamate inhibition of NMDA → increases pathway activity → treats Alzheimer's
MigrateNegative → migrates toward anode (+)
Glu
Glutamate
Acidic
ChargeNegative — extra COO⁻
FunctionMain excitatory neurotransmitter in the brain
LinkGlutamate → GABA (via glutamate decarboxylase). The GABA connection is huge — see below.
MigrateNegative → migrates toward anode (+)
💥 Sulfur-Containing Disulfide bonds
Cys
Cysteine
Sulfur • Disulfide King
ContainsSulfur — has the MOST sulfur of any amino acid
FunctionMakes disulfide bonds (S—S) — critical for protein folding and stability
Board Hit4 hormones with lots of disulfide bonds: "PIGI"Prolactin, Insulin, Growth Hormone, Inhibin 🔑PIGI — like a piggy bank: Prolactin, Insulin, Growth Hormone, Inhibin. All held together by disulfide bonds from cysteine.
Met
Methionine
Sulfur • Essential
ContainsSulfur
FunctionAlso makes disulfide bonds
SpecialStart codon (AUG) codes for Met — first amino acid in every protein
🔗 Amide Amino Acids N-linked bonds • end in "-ine"
Asn
Asparagine
Amide
BondsInvolved in N-linked bonds (glycosylation)
RememberEnds in "-ine" → has an extra amine group (NH₂)
Gln
Glutamine
Amide
BondsInvolved in N-linked bonds
FunctionMajor fuel for enterocytes (intestinal cells) and immune cells
RememberEnds in "-ine" → extra amine group
💧 Hydroxyl Amino Acids O-linked bonds • extra -OH
Ser
Serine
Hydroxyl
BondsInvolved in O-linked bonds
SpecialFound in the active site of many enzymes (serine proteases: trypsin, chymotrypsin, elastase, thrombin)
ExtraHas extra -OH group → phosphorylation target for kinases
Thr
Threonine
Hydroxyl • Essential
BondsInvolved in O-linked bonds
ExtraHas extra -OH group
EnergyBoth glucogenic AND ketogenic
💪 Branched-Chain Amino Acids (BCAAs) Can't "LIV" without them
Leu
Leucine
BCAA • Essential
EnergyPurely KETOGENIC — one of only 2 (Lys + Leu)
TransportAll 3 BCAAs share the same transport protein in the collecting duct of the kidney
Iso
Isoleucine
BCAA • Essential
EnergyBoth glucogenic AND ketogenic
TransportShares transport protein with Leu and Val
Val
Valine
BCAA • Essential
DiseaseMaple syrup urine disease — can't break down BCAAs → sweet-smelling urine
EnzymeBranched-chain amino acid dehydrogenase needs 5 vitamins (same as pyruvate DH and α-ketoglutarate DH)
Ketogenic vs Glucogenic Summary
Purely Ketogenic (2 only)
Lysine and Leucine

Ketogenic = broken down into acetyl-CoA → used to make ketones

Can NOT be used to make glucose
Both Glucogenic & Ketogenic (4)
PHE, ISO, THR, TRP

Can go both ways — broken down into intermediates that feed into gluconeogenesis OR ketogenesis 🔑"PITT" — PHE, ISO, THR, TRP. Like Brad Pitt — he can play any role (glucogenic or ketogenic).
🧠 The GABA Connection
NH₄⁺ + αKG → Glutamate → GABA
Ammonium (NH₄⁺) comes from urea and acid: NH₃ + H⁺ = NH₄⁺

The Le Chatelier principle: increase things on the right → shifts left. Increase things on the left → shifts right → more glutamate → more GABA.

GABA is inhibitory — more GABA = things slow down. This is the key link:
Liver failure → can't clear ammonia → ↑NH₄⁺ → ↑glutamate → ↑GABA → hepatic encephalopathy (patient slows down, becomes comatose)
Kidney failure → can't clear urea → ↑urea → same pathway → uremic encephalopathy
DKA → ketones are acidic → ↑acid → ↑NH₄⁺ → ↑GABA → diabetic coma
Any disease with high acid, urea, or ammonia will increase GABA → patients go to sleep/coma but do not wake up
Enzyme Recognition Cheat Sheet
EnzymeRecognizesAction
ChymotrypsinPHE, TRP, TYR (aromatics)Cuts to their right side
TrypsinLYS, ARG (basic)Cuts to their right side
Serine proteasesHave Ser in active siteTrypsin, chymotrypsin, elastase, thrombin
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