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Literature summary for 4.98.1.1 extracted from

  • Sudhamsu, J.; Kabir, M.; Airola, M.V.; Patel, B.A.; Yeh, S.R.; Rousseau, D.L.; Crane, B.R.
    Co-expression of ferrochelatase allows for complete heme incorporation into recombinant proteins produced in E. coli (2010), Protein Expr. Purif., 73, 78-82.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.98.1.1

Application

Application Comment Organism
biotechnology co-expression with ferrochelatase along with the addition of a small amount of delta-aminolevulinic acid, is sufficient to produce fully incorporated heme protein. This method is applicable for both Cys-ligated and His-ligated heme proteins Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
co-expression of just one native protein, ferrochelatase, in the presence of 60 microM delta-aminolevulinic acid (10 mg/l) is sufficient for 100% heme incorporation into three unrelated heme proteins derived from different organisms Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrin IX + Fe2+ Escherichia coli
-
 protoheme IX + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin IX + Fe2+
-
 Escherichia coli protoheme IX + 2 H+
-
 ?

Synonyms

Synonyms Comment Organism
FeCH
-
 Escherichia coli
ferrochelatase
-
 Escherichia coli