4.2.1.165: chlorophyllide a 31-hydratase
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For detailed information about chlorophyllide a 31-hydratase, go to the full flat file.
Reaction
Synonyms
2-vinyl bacteriochlorophyllide hydratase, 3-vinyl bacteriochlorophyllide a hydratase, 3-vinyl hydratase, 3-vinyl-bacteriochlorophyll hydratase, 31-hydratase, bacterial 3-vinyl hydratase, bchF, BchF hydratase, Cabther_B0080, cfxBchF, ClimR0003, ClimR0008, ClimR0017, craBchF, CT1421
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Engineering
Engineering on EC 4.2.1.165 - chlorophyllide a 31-hydratase
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additional information
deletion of gene bchF in a BChl b-producing strain of Rhodobacter sphaeroides leads to the production of an analogue of bacteriochlorophyllide g, BChl gP, where P is phytyl, rather than the native BChl aP. In the bchF-deletion mutant, hydration of the C3-vinyl group in 3-vinyl bacteriochlorophyllide a is blocked, but this precursor can be esterified with phytol. Enzyme BchF deletion- in the DELTAbciA/bchXYZBv background results in formation of BChl g esterified with phytol (BChl gP)
additional information
bchF deletion mutant, mutant phenotype with altered pigment biosynthesis, detailed overview
additional information
reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
additional information
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reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
additional information
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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reconstitution of a bacteriochlorophyll formation pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC, with chlorin 3-hydroxyethyl chlorophyllide as a natural substrate identified for BchC. Modification of the isocyclic E ring, omission of the central magnesium ion, zinc as an alternative metal ion, and a non-reduced B ring system are tolerated by BchC. According to this broadened in vitro activity, the chlorin 3-hydroxyethyl chlorophyllide a is identified as a natural substrate of BchC in a reconstituted pathway consisting of dark-operative protochlorophyllide oxidoreductase, BchF, and BchC. The established reaction sequence allows for an additional new branching point for the synthesis of bacteriochlorophyll a
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additional information
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
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bchF deletion mutant, mutant phenotype with altered pigment biosynthesis, detailed overview
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