Information on EC 4.2.1.169 - 3-vinyl bacteriochlorophyllide d 31-hydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.169
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RECOMMENDED NAME
GeneOntology No.
3-vinyl bacteriochlorophyllide d 31-hydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 3-(1-hydroxyethyl) bacteriochlorophyllide d = a 3-vinyl bacteriochlorophyllide d + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacteriochlorophyll c biosynthesis
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bacteriochlorophyll d biosynthesis
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bacteriochlorophyll e biosynthesis
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Porphyrin and chlorophyll metabolism
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
3-vinylbacteriochlorophyllide-d 31-hydro-lyase
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is involved in the biosynthesis of bacteriochlorophylls c, d and e. It acts in the direction of hydration, and the hydroxyl group that is formed is essential for the ability of the resulting bacteriochlorophylls to self-aggregate in the chlorosomes, unique light-harvesting antenna structures found in these organisms. The product is formed preferentially in the (R)-configuration.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a 3-vinyl bacteriochlorophyllide a + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide a
show the reaction diagram
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
show the reaction diagram
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
show the reaction diagram
zinc 3-vinyl-8-ethyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
show the reaction diagram
zinc 3-vinyl-8-propyl-12-methyl-bacteriopheophorbide c + H2O
zinc 31R-bacteriopheophorbide c + zinc 31S-bacteriopheophorbide c
show the reaction diagram
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
a 3-vinyl bacteriochlorophyllide d + H2O
a 3-(1-hydroxyethyl) bacteriochlorophyllide d
show the reaction diagram
chlorophyllide a + H2O
3-devinyl-3-(1-hydroxyethyl)-chlorophyllide a
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the central metal of substrates is essential for the BchF reaction; the central metal of substrates is essential for the BchV reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bchF quantitative RT-PCR expression analysis, phylogenetic analysis; gene bchV, quantitative RT-PCR expression analysis, phylogenetic analysis
gene bchV, the enzyme is encoded upstream of, but divergently oriented from, bchQ (which encodes the BChl c-specific C-82 methyltransferase)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcriptional level of bchV gene is upregulated under low light conditions
transcriptional level of bchV is upregulated at lower light intensity, the Chlorobaculum tepidum adapts to low-light environments by control of the bchV transcription
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information