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Results 1 - 10 of 27 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93N222D autocatalytic and neuropeptide processing is impaired 687032
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more carboxyl terminus-truncated PC3 (1-638) containing the transmembrane domain is associated with lipid rafts in Neuro2A cells, while PC3 (1-616) and PC3-deltaTM lacking the transmembrane domain are not. PC3 (1-638) undergoes stimulated secretion and is colocalized with the secretory granule marker, chromogranin A, by immunocytochemistry. In contrast, PC3 (1-616) and PC3-deltaTM are constitutively secreted and primarily localized in the Golgi 688980
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more concentration of progastrin in the antrum of PC1/3-null mice is elevated 3fold. Progastrin molecule is only partly cleaved at the dibasic Arg36-Arg37 site and even less at the Lys53-Lys54 site in the PC1/3-null mice 696097
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more construction of an PC3 containing a 19 amino-acid transmembrane sequence, and/or a C-terminal glycosylation tag, the C-terminal extension is exposed to the endoplasmic reticulum lumen, overview 667660
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more construction of PC1 prosegment, amino acids 1-110, fused to the C-terminal PC1 tail, amino acids 619-753, termed proCT construct 668621
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more design of prohormone convertase-2-specific mutations into the catalytic domain of PC1/3 in order to investigate the molecular contributions of these sequences to PC1/3-specific properties. The exchange of residues RQG314 with the SY sequence present in the same location within PC2 shifts the pH optimum of PC1/3 upward into the neutral range, other mutations in the catalytic domain had no effect. None of the full-length PC1/3 mutants examined exhibits increased specific activity, but the 66-kDa form of the RQG314SY mutant is 2 to 4 times more active than the 66-kDa form of wild-type PC1/3. Mutation of GIVTDA243–248 to QPFMTDI, a molecular determinant of 7B2 binding, results in increased zymogen expression but no propeptide cleavage or secretion, suggesting that this mutant is trapped in the endoplasmic reticulum. None of the mutations examined confers PC2-specific properties. No mutant exhibits altered calcium requirements 717543
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more generation of chimeric PC1-propeptide/SAAS CT peptide constructs, effects on C-terminal PC1 processing are limited to the construct containing the PC1 propeptide alone when expressed in AtT20 cells, while both the PC1 propeptide and the SAAS CT propeptide are inhibitory on C-terminal PC1 zymogen processing when expressed in HEK293 cells, overview 669648
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93more identification of polymorphisms of the PC1 gene in 447 individuals from three breeds. Only the P1, P2, P3, P9, and P10 loci show polymorphisms, and 12 SNPs in the PC1 gene have been identified. The polymorphisms are significantly associated with caprine body height and chest circumference 717206
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93N222D leads to obesity, abnormal proinsulin processing, reduced fecundity, impaired autocatalysis and multiple endocrinological defects in mice homozygous for the mutation. Increased energy intake, a more efficient metabolism and reduced alpha-MSH signaling contribute to the obesity. Heterozygous littermates exhibit an intermediate phenotype for both sexes, thus this mutation results in a semi-dominant phenotype -, 687032
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.93S357G mutant represents a prohormone convertase PC1/3 hypermorph. Mutant protein exhibits a lower calcium dependence, a higher pH optimum, and a higher resistance to peptide inhibitors than the wild-type enzyme. The mutant exhibits increased cleavage to the C-terminally truncated form, and kinetic parameters of the full-length and truncated mutant enzymes are also altered. The S357G mutation broadens the specificity of the enzyme, it displays proprotein convertase 2-like specificity on the substrate proCART, the precursor of the cocaine- and amphetamine regulated transcript neuropeptide. The mutant enzyme possesses unusual processing activity that may significantly change the profile of circulating peptide hormones 731721
Results 1 - 10 of 27 > >>