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Literature summary for 3.4.21.93 extracted from

  • Ozawa, A.; Peinado, J.R.; Lindberg, I.
    Modulation of prohormone convertase 1/3 properties using site-directed mutagenesis (2010), Endocrinology, 151, 4437-4445.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in HEK-293 and PC-12 cell Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information 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 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-neurotensin + H2O
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Mus musculus ?
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?

Synonyms

Synonyms Comment Organism
PC1/3
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Mus musculus
prohormone convertase 1/3
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Mus musculus