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Information on EC 4.99.1.4 - sirohydrochlorin ferrochelatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15807

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IUBMB Comments
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
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Saccharomyces cerevisiae
UNIPROT: P15807
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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siroheme
+
2
H+
=
sirohydrochlorin
+
Fe2+
+
2
=
+
Synonyms
sirohydrochlorin ferrochelatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Met8p
Saccharomyces cerevisiae
CysG
-
-
-
-
Met8p
SirB
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
siroheme + 2 H+ = sirohydrochlorin + Fe2+
show the reaction diagram
the enzyme from Pseudomonas chloroaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity, the enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate, no activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime, mechanism
-
SYSTEMATIC NAME
IUBMB Comments
siroheme ferro-lyase (sirohydrochlorin-forming)
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-93-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
show the reaction diagram
-
-
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
sirohydrochlorin + Fe2+
siroheme + H+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme
-
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
show the reaction diagram
-
Met8p catalyzes ferrochelation during the biosynthesis of siroheme
-
?
sirohydrochlorin + Fe2+
siroheme + H+
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0311
wild-type Met8p
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
three structural domains per monomer, domain structure
homodimer
-
each monomer is composed of three functional domains, domain structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray crystal structure of Met8p
-
X-ray crystal structure of Met8p, hanging drop method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D141A
mutant of bifunctional Met8p is completely inactive as both dehydrogenase and ferrochelatase
G22D
mutant of bifunctional Met8p is completely inactive as dehydrogenase, but functions as ferrochelatase
H237A
mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase
D141A
-
mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities
G22D
-
mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schubert, H.L.; Raux, E.; Brindley, A.A.; Leech, H.K.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase
EMBO J.
21
2068-2075
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P15807)
Manually annotated by BRENDA team
Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase
Biochem. Soc. Trans.
30
595-600
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team