CreatinevsNALT

Creatine is phosphorylated by mitochondrial creatine kinase (CK-Mt) to form phosphocreatine (PCr), which serves as a rapidly mobilizable high-energy phosphate reserve. When neuronal ATP is consumed during demanding tasks (synaptic vesicle cycling, ion pump activity, action potential propagation), cytosolic brain-type creatine kinase (CK-BB) catalyzes the transfer of the phosphoryl group from PCr to ADP, regenerating ATP within milliseconds — far faster than oxidative phosphorylation or glycolysis can respond. This PCr/CK shuttle also transports high-energy phosphates from mitochondria to distant synaptic sites. Creatine provides direct neuroprotection by stabilizing the mitochondrial permeability transition pore (mPTP), preventing cytochrome c release and downstream apoptotic cascades. It scavenges reactive oxygen species by acting as a direct antioxidant against superoxide and peroxynitrite. Creatine also increases GLUT4 expression in neurons, improving glucose uptake, and upregulates brain-derived neurotrophic factor (BDNF) expression in the hippocampus, supporting synaptic plasticity and memory consolidation.

NALT (N-acetyl L-tyrosine) is deacetylated by aryl acylamidase in the gut and liver to release L-Tyrosine. Tyrosine is hydroxylated to L-DOPA by tyrosine hydroxylase (TH) — the rate-limiting step in catecholamine synthesis, requiring tetrahydrobiopterin as cofactor. L-DOPA is decarboxylated by aromatic L-amino acid decarboxylase (AADC) to dopamine; dopamine is converted to norepinephrine by dopamine beta-hydroxylase (DBH), and norepinephrine to epinephrine by phenylethanolamine N-methyltransferase (PNMT). Under stress or sleep deprivation, catecholamine stores in noradrenergic and dopaminergic neurons deplete rapidly. Supplemental tyrosine provides substrate to maintain synthesis when demand exceeds supply, supporting prefrontal cortex function and working memory.