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

BRENDA support

Literature summary extracted from

  • Medlock, A.E.; Dailey, T.A.; Ross, T.A.; Dailey, H.A.; Lanzilotta, W.N.
    A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase (2007), J. Mol. Biol., 373, 1006-1016.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.98.1.1 additional information conformational changes in a structurally conserved phi-helix that is predicted to have a central role in product release Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.98.1.1
-
 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.98.1.1 crystals of wild-type enzyme in the presence of ammonium chloride or manganese chloride, wild-type enzyme adopts a predominantly open conformation Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.98.1.1 E343K upper lip of the active site is altered in spatial orientation in the E343K substrate-bound mutant relative to the wild-type enzyme structure Homo sapiens
4.98.1.1 F110A unaltered Km values, but with a diminished Kcat with respect to wild-type enzyme Homo sapiens
4.98.1.1 R115L Kcat is slightly lower than that of wild-type, but the Km for porphyrin is slightly higher Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.98.1.1 Pb2+
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.98.1.1 0.02
-
 Fe2+ mutant F110A Homo sapiens
4.98.1.1 0.021
-
 Fe2+ mutant R115L Homo sapiens
4.98.1.1 0.07
-
 Fe2+ wild-type Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.98.1.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.98.1.1
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.98.1.1 protoporphyrin IX + Fe2+ enzyme undergoes significant changes in secondary structure during the catalytic cycle Homo sapiens protoheme IX + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.98.1.1 protoheme ferrolyase
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.98.1.1 0.018
-
 Fe2+ wild-type Homo sapiens
4.98.1.1 0.053
-
 Fe2+ mutant F110A Homo sapiens
4.98.1.1 0.053
-
 Fe2+ mutant R115L Homo sapiens