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Literature summary for 3.4.17.2 extracted from

  • Son, Y.J.; Kim, C.K.; Kim, Y.B.; Kweon, D.H.; Park, Y.C.; Seo, J.H.
    Effects of citraconylation on enzymatic modification of human proinsulin using trypsin and carboxypeptidase B (2009), Biotechnol. Prog., 25, 1064-1070.
    View publication on PubMed
Search for more literature for 3.4.17.2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
human proinsulin + H2O Sus scrofa enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process is developed for the reduction of a major derivative, des-threonine human insulin ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human proinsulin + H2O enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process is developed for the reduction of a major derivative, des-threonine human insulin Sus scrofa ?
-
 ?

Synonyms

Synonyms Comment Organism
carboxypeptidase B
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
 assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Sus scrofa