tripeptidyl peptidase

tripeptidyl peptidase

(1) Tripeptidyl-peptidase I, EC 3.4.14.9. 
(2) Tripeptidyl-peptidase II, EC 3.4.14.10.
References in periodicals archive ?
In April 2017, the company received the second voucher following approval of Brineura, a new biological product for patients with late infantile neuronal ceroid lipofuscinosis type 2 (CLN2), also known as tripeptidyl peptidase 1 (TPP1) deficiency, a form of Batten disease.
A form with mostly infantile manifestation (CLN1) and the classical late infantile form (CLN2) are caused by deficiencies of the lysosomal enzymes palmitoyl protein thioesterase 1 (PPT1) and tripeptidyl peptidase 1 (TPP1), respectively.
In infantile and late infantile NCL, the disorder is brought on by inherited mutations in the CLN1 gene, which codes for palmitoyl-protein thioesterase 1 (PPT1) or in the CLN2 gene, which codes for tripeptidyl peptidase I (TPP-I), respectively.
Additionally, LINCL is caused by mutations in the Cln2 gene that leads to the deficiency and/or loss of function of Tripeptidyl Peptidase 1 (TPP1) that leads to accumulation of autofluorescent storage materials in neurons and in other cells.
The recent realization that the CLN2 protein is identical to the lysosomal enzyme tripeptidyl peptidase I (TPP-I) (10-12) should simplify detection of CLN2 deficiencies because this assay is simpler and uses a commercially available substrate.
Although there also exists a neutral tripeptidyl peptidase, experiments investigating the pH dependence of tripeptidyl peptidase activity in control and LINCL leukocytes, lymphoblasts, fibroblasts, and brain indicated that it did not contribute to the CLN2-derived activity at pH 4.
s (NASDAQ: BMRN) Brineura (cerliponase alfa), the first treatment approved in the European Union for the treatment of neuronal ceroid lipofuscinosis type 2, also known as tripeptidyl peptidase 1 deficiency, the company said.
The request concerns Bio Marin's BMN-190, an investigational recombinant human tripeptidyl peptidase 1 for the treatment of Batten disease, or neuronal ceroid lipofuscinosis type 2 (NCL-2).
In the infantile and late infantile subtypes of NCL, the disorder is brought on by inherited mutations in the CLN1 gene, which codes for palmitoyl-protein thioesterase 1 (PPT1) or in the CLN2 gene, which codes for tripeptidyl peptidase I (TPP-I), respectively.
In two subtypes of NCL, infantile and late infantile, the disorder is brought on by inherited mutations in the CLN1 gene, which codes for palmitoyl-protein thioesterase 1 (PPT1) or in the CLN2 gene, which codes for tripeptidyl peptidase I (TPP-I).
In two subtypes of the NCLs, infantile and late infantile NCL, the disorders are brought on by inherited genetic mutations in the CLN1 gene, which codes for palmitoyl-protein thioesterase 1 (PPT1) and in the CLN2 gene, which codes for tripeptidyl peptidase I (TPP-I).
NCLs are lysosomal storage disorders brought on by inherited genetic mutations in CLN1 gene, which codes for palmitoyl-protein thioesterase 1 (PPT1) and in the CLN2 gene, which codes for tripeptidyl peptidase I (TPP-I).