Information on EC 1.3.7.15 - chlorophyllide a reductase

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The expected taxonomic range for this enzyme is: Rhodobacteraceae

EC NUMBER
COMMENTARY hide
1.3.7.15
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RECOMMENDED NAME
GeneOntology No.
chlorophyllide a reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(3)
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3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(1)
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bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacteriochlorophyll a biosynthesis
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Biosynthesis of secondary metabolites
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase
The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) [4]. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Rubrobacter radiotolerans
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Manually annotated by BRENDA team
no activity in Rubrobacter xylanophilus
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
show the reaction diagram
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
show the reaction diagram
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?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
show the reaction diagram
protochlorophyllide + reduced dithionite + ATP + H2O + H+
chlorophyllide a + oxidized dithionite + ADP + phosphate
show the reaction diagram
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?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
show the reaction diagram
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?
additional information
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
show the reaction diagram
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
show the reaction diagram
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?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
show the reaction diagram
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protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
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[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 53000 + x * 56000 + x * 53000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is labile in the presence of O2
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-loaded chelating Sepharose column chromatography
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Strep-Tactin, column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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reconstitution of chlorophyllide a reductase with purified proteins. Two Rhodobacter capsulatus strains that overexpress Strep-tagged BchX and BchY are isolated. Strep-tagged BchX is purified as a single polypeptide, and BchZ is co-purified with Strep-tagged BchY. When BchX and BchY-BchZ components are incubated with chlorophyllide a, ATP, and dithionite under anaerobic conditions, chlorophyllide a is converted to a new pigment
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C145A
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the mutant of subunit BchY is inactive
C35A
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the mutant of subunit BchZ is inactive
C35D
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the mutant of subunit BchZ is inactive; the mutant of subunit BchZ shows 60% of wild type activity
C35D/S94C
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the mutant of subunit BchZ is inactive
C35S
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the mutant of subunit BchZ is inactive
C62A
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the mutant of subunit BchY is inactive
C86A
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the mutant of subunit BchY shows 50% of wild type activity
C87A
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the mutant of subunit BchY is inactive