Homocarnosinase: A hog kidney dipeptidase with a broader specificity than carnosinase

• Published in: Archives of biochemistry and biophysics Vol. 184; no. 1; pp. 257 - 266
• Main Authors: Lenney, James F., Kan, Siu-Chow, Siu, Kingsum, Sugiyama, Glen H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.11.1977
• Subjects: Animals; Carnosine - analogs & derivatives; Cobalt - pharmacology; Dipeptidases - isolation & purification; Dipeptidases - metabolism; Hydrogen-Ion Concentration; Kidney - enzymology; Kinetics; Rats; Substrate Specificity; Swine; Tissue Distribution
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1016/0003-9861(77)90349-6

A dipeptidase was isolated from hog kidney; it is the first enzyme described that has the capacity to cleave homocarnosine. It was purified to apparent homogeneity and split carnosine, anserine, and several other dipeptides in addition to homocarnosine. Homocarnosinase had a molecular weight of 57,000 as determined by sodium dodecyl sulfate-gel electrophoresis; it appeared to consist of a single polypeptide chain and did not contain sulfhydryl groups or serine residues essential to its activity. The enzyme was activated by Co 2+ and by Mn 2+, cobaltous ions being much more effective than manganous ions. Its isoelectric point was 5.6 and no evidence of isozymes was seen during isoelectric focusing. Homocarnosinase had a broader specificity, higher solubility, lower stability, and different metal ion sensitivity than hog kidney carnosinase (EC 3.4.13.3). Carnosinase was present in most tissues of the rat, whereas homocarnosinase was detected only in kidney, uterus, lung, and liver.