Literature summary for 4.99.1.9 extracted from

Hansson, M.D.; Karlberg, T.; Rahardja, M.A.; Al-Karadaghi, S.; Hansson, M.
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX (2007), Biochemistry, 46, 87-94.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in presence of iron. Only a single iron ion is found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron ion is not present in the structure of a His183Ala modified ferrochelatase. Insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264	Bacillus subtilis

Crystallization (Comment)

Organism

structure in presence of iron. Only a single iron ion is found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron ion is not present in the structure of a His183Ala modified ferrochelatase. Insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264

Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
E264Q	21% of wild-type activity	Bacillus subtilis
E264V	less than 1% of wild-type activity	Bacillus subtilis
H183A	less than 1% of wild-type activity	Bacillus subtilis
H183C	less than 1% of wild-type activity	Bacillus subtilis
H88A	5% of wild-type activity	Bacillus subtilis
K87A	92% of wild-type activity	Bacillus subtilis
Y13F	71% of wild-type activity	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P32396	-	-
Bacillus subtilis 168	P32396	-	-

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Release 2023.1 (January 2023)