Specificity and distribution of mammalian carnosinase.
Hog kidney carnosinase (EC 3.4.13.3) was found to have a narrow specificity; it hydrolyzed carnosine, anserine and glycyl-L-histidine, but did not split L-alanyl-L-histidine or homocarnosine. The isoelectric point of this enzyme was 5.8 and its molecular weight was about 84 000. Carnosinase was found to be widely distributed in various tissues of the rat. Uterus, kidney, liver and lung contained high levels of carnosinase, whereas moderate concentrations were found in spleen, heart and brain, with low levels in small intestine, skeletal muscle and stomach, and none in blood.
D000818:Animals; D002336:Carnosine / Q000378:metabolism; D004150:Dipeptidases / Q000378:metabolism*; D005260:Female; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008970:Molecular Weight; D009928:Organ Specificity; D051381:Rats; D013329:Structure-Activity Relationship; D013552:Swine; D014599:Uterus / Q000201:enzymology
D002336:Carnosine; D004150:Dipeptidases; C019673:aminoacyl-histidine dipeptidase