Carnosine (dipeptide)

Higher levels can be due to deficiency of enzyme carnosinase or its cofactor, zinc. This analyte is a ß-alanyl dipeptide of histidine.

– Inherited carnosinase enzyme deficits lead to neurological development problems and sensory polyneuropathy.

– Breakdown of Carnosine requires a zinc dependent peptidase, which can be inhibited by high levels of the ”end product” beta-alanine. Zinc status should be checked (RBC Elements) since the peptidase activity is zinc dependent. The peptidase activity can also be inhibited by high levels of Beta-alanine, which can result from B-6 insufficiency, or abnormal intestinal flora.

– Beta-alanine can accumulate if deamination of beta-alanine to alpha-ketoglutarate is impaired due to B-6 insufficiency. Therefore, carnosine can accumulate as a result of high intake of carnosine containing meats (beef, pork, tuna and salmon) with insufficient zinc and/or B-6 availability.

– Beta-alanine can also be elevated as a product of gastrointestinal bacterial conversion of aspartate and/or breakdown of pyrimidines that are high in yeast. Thus beta-alanine can accumulate and inhibit hydrolysis of carnosine as a result of significant dysbiosis, or deficiencies of B-6 and/or zinc.

Carnosine, a dietary peptide, is measured to be lower than the reference range. Carnosine comes from certain meat and fish protein. It is typically low or absent for individuals who eat low protein diets or who follow vegetarian or vegan diets. There is no clinical significance for low carnosine.

Carnosine is a dietary peptide related marker that consists of histidine and beta-alanine. Carnosine is an incompletely digested peptide that is derived primarily from beef and pork.