Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.17.2 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

EC Number Organism UniProt Comment Textmining
3.4.17.2 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.17.2 pancreas
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.17.2 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

EC Number Synonyms Comment Organism
3.4.17.2 carboxypeptidase B
-
 Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.17.2 15
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.17.2 8.5
-
 assay at Sus scrofa