EC Number   |
General Information |
Reference |
|---|
  4.2.1.165 | evolution |
genotyping of single copy gene encoding BchF in Proteobacteria, Acidobacteria, Chloroflexi, and Gemmatimonadetes. Phototrophic Chlorobi usually carry two or three paralogues of BchF, with a second form named BchV. The different versions of BchF in Chlorobi are thought to aid in the synthesis of enantiomeric forms of bacteriochlorophyll c, d, and e that are characteristic of this phylum. Bacteriochlorophyll a cannot be synthetized without BchF and because BchF is only and exclusively found in those bacteria that make bacteriochlorophyll a, the phylogeny of this enzyme is, in consequence, the most direct piece of evidence for the origin of phototrophy based on bacteriochlorophyll a. Phylogenetic analysis, overview. The ancestral form of BchF originated early during the evolution of bacteria at a point in time that predated the diversification of the major groups of anoxygenic phototrophs |
749080 |
| 4.2.1.165 | malfunction |
deletion of bchF gene affects the composition of 31R/S-epimers in composite BChls c: the bchF-deleted mutant has nearly 100% R-stereochemistry in [E,M]- and [E,E]BChl c, 9-12% S-stereochemistry in [P,E]BChl c, and nearly 100% S-stereochemistry in [I,E]BChl c |
748858 |
| 4.2.1.165 | malfunction |
deletion of gene bchF in a bacteriochlorophyll (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). Pigment analysis in several bch mutants, overview |
747177 |
| 4.2.1.165 | malfunction |
further methylation at the 82- and 20-positions suppresses the in vitro hydration of the 3-vinyl group by the BchF/V hydratases. In vivo experiments with bchF-deleted mutants show considerably lower levels of bacteriochlorophyll a than the wild-type strain |
-, 748860 |
| 4.2.1.165 | malfunction |
pigment analyses of the bchF-inactivated mutant, which still has BchV as a sole hydratase, show higher ratios of S-epimeric bacteriochlorophyll c than the wild-type strain, while the bchV-mutant possessing only BchF showed a significant decrease of the S-epimers and accumulations of C3-vinyl BChl c species. In BChl a biosynthesis, the C3-vinyl group of a precursor of BChl a is hydrated by BchF, and the C3-1-hydroxyethyl group is then oxidized to the acetyl moiety by BchC |
-, 748684 |
| 4.2.1.165 | metabolism |
BchF may specifically be required for bacteriochlorophyll a biosynthesis |
-, 741110 |
| 4.2.1.165 | metabolism |
enzyme involvement in the biosynthetic pathways of BChl c homologues and epimers, overview |
748858 |
| 4.2.1.165 | metabolism |
proposed biosynthetic pathways of bacteriochlorophyllides a and c focused on Chlorobaculum tepidum BchF- and BchV-catalyzed reactions, overview |
-, 748684 |
| 4.2.1.165 | metabolism |
the enzyme is involved in the biosynthetic pathways of different baceriochlorophyllides, e.g. a and g, overview |
747177 |
| 4.2.1.165 | physiological function |
a bacteriochlorophyll-less mutant of Rhodopseudomonas sphaeroides excretes tetrapyrrole-protein complex into the incubation medium. The major pigment of the complex is 2-desacetyl-2-vinylbacteriopheophorbide, indicating the existence of an alternate pathway of bacteriochlorophyll synthesis. This implies that reduction from the chlorin to the tetrahydroporphyrin stage can occur either before or after hydration of the 2-vinyl substituent of chlorophyllide a to an a-hydroxyethyl group. The mutant is presumably deficient in the enzyme responsible for hydration of the 2-vinyl to the 2-alpha-hydroxyethyl group |
737663 |
