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Literature summary for 1.14.11.2 extracted from

  • Shi, J.; Ma, X.; Gao, Y.; Fan, D.; Zhu, C.; Mi, Y.; Xue, W.
    Hydroxylation of human type III collagen alpha chain by recombinant coexpression with a viral prolyl 4-hydroxylase in Escherichia coli (2017), Protein J., 36, 322-331 .
    View publication on PubMed

Application

Application Comment Organism
synthesis viral P4H (A085R) is coexpressed as a soluble and active monomer in Escherichia coli with full-length human collagen alpha1(III) chain (COL3A1). This coexpression system can be used for the production of hydroxylated human collagen alpha1(III) chain (COL3A1) in Escherichia coli. The method avoids the complexity of P4H assembly Paramecium bursaria Chlorella virus 1

Cloned(Commentary)

Cloned (Comment) Organism
expression by Escherichia coli BL21(DE3) Paramecium bursaria Chlorella virus 1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2 Paramecium bursaria Chlorella virus 1
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procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Paramecium bursaria Chlorella virus 1 Q84406
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen L-proline + 2-oxoglutarate + O2
-
Paramecium bursaria Chlorella virus 1 procollagen trans-4-hydroxy-L-proline + succinate + CO2
-
?

Synonyms

Synonyms Comment Organism
A085R
-
Paramecium bursaria Chlorella virus 1
prolyl 4-hydroxylase A085R
-
Paramecium bursaria Chlorella virus 1