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Literature summary for 4.98.1.1 extracted from

  • Storm, P.; Tibiletti, T.; Hall, M.; Funk, C.
    Refolding and enzyme kinetic studies on the ferrochelatase of the cyanobacterium Synechocystis sp. PCC 6803 (2013), PLoS ONE, 8, e55569.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.98.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta 2 (DE3) cells Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
FeChDELTA347 removal of the C-terminal CAB-domain led to a greatly increased turnover number, kcat, compared to the full length protein Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
additional information the presence of pigments results in lower enzyme activity Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00022
-
 protoporphyrin IX wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C Synechocystis sp.
0.0003
-
 protoporphyrin IX mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C Synechocystis sp.
0.000488
-
 Zn2+ wild type enzyme, at pH 8.0 and 30°C Synechocystis sp.
0.000836
-
 Zn2+ mutant enzyme FeChDELTA347, at pH 8.0 and 30°C Synechocystis sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Synechocystis sp. P54225
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-IMAC column chromatography and Sephacryl S-300 gel filtration Synechocystis sp.

Renatured (Commentary)

Renatured (Comment) Organism
using 50 mM Tris pH 8, 3 M guanidinium hydrochloride, 0.1 M NaCl and 0.1 mM Tris (2-carboxyethyl) phosphine Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrin IX + Fe2+
-
 Synechocystis sp. protoheme IX + 2 H+
-
 ?
protoporphyrin IX + Zn2+
-
 Synechocystis sp. ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Synechocystis sp.

Synonyms

Synonyms Comment Organism
FeCH
-
 Synechocystis sp.
protohaem ferrolyase
-
 Synechocystis sp.
type II ferrochelatase
-
 Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.034
-
 Zn2+ wild type enzyme, at pH 8.0 and 30°C Synechocystis sp.
0.049
-
 Zn2+ mutant enzyme FeChDELTA347, at pH 8.0 and 30°C Synechocystis sp.
0.052
-
 protoporphyrin IX wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C Synechocystis sp.
0.073
-
 protoporphyrin IX mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Synechocystis sp.

General Information

General Information Comment Organism
metabolism ferrochelatase is the key enzyme in the heme biosynthesis pathway Synechocystis sp.