Enzymes
| UniProtKB help_outline | 117 proteins |
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- Name help_outline 15,16-dihydrobiliverdin Identifier CHEBI:57899 Charge -2 Formula C33H34N4O6 InChIKeyhelp_outline ZQHDSLZHMAUUQK-ZTYGKHTCSA-L SMILEShelp_outline [H][C@]1(CC2=N\C(=C/c3[nH]c(\C=C4NC(=O)C(C)=C/4C=C)c(C)c3CCC([O-])=O)\C(CCC([O-])=O)=C2C)NC(=O)C(C=C)=C1C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
oxidized 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10004
Reactive part
help_outline
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline biliverdin IXα Identifier CHEBI:57991 Charge -2 Formula C33H32N4O6 InChIKeyhelp_outline QBUVFDKTZJNUPP-BBROENKCSA-L SMILEShelp_outline C=1(/C=C/2\NC(=O)C(=C2C=C)C)NC(=C(C1C)CCC([O-])=O)/C=C/3\N=C(/C=C/4\NC(C(=C4C)C=C)=O)C(=C3CCC([O-])=O)C 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
reduced 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10002
Reactive part
help_outline
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:10168 | RHEA:10169 | RHEA:10170 | RHEA:10171 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms.
Frankenberg N., Mukougawa K., Kohchi T., Lagarias J.C.
Phytobilins are linear tetrapyrrole precursors of the light-harvesting prosthetic groups of the phytochrome photoreceptors of plants and the phycobiliprotein photosynthetic antennae of cyanobacteria, red algae, and cryptomonads. Previous biochemical studies have established that phytobilins are sy ... >> More
Phytobilins are linear tetrapyrrole precursors of the light-harvesting prosthetic groups of the phytochrome photoreceptors of plants and the phycobiliprotein photosynthetic antennae of cyanobacteria, red algae, and cryptomonads. Previous biochemical studies have established that phytobilins are synthesized from heme via the intermediacy of biliverdin IX alpha (BV), which is reduced subsequently by ferredoxin-dependent bilin reductases with different double-bond specificities. By exploiting the sequence of phytochromobilin synthase (HY2) of Arabidopsis, an enzyme that catalyzes the ferredoxin-dependent conversion of BV to the phytochrome chromophore precursor phytochromobilin, genes encoding putative bilin reductases were identified in the genomes of various cyanobacteria, oxyphotobacteria, and plants. Phylogenetic analyses resolved four classes of HY2-related genes, one of which encodes red chlorophyll catabolite reductases, which are bilin reductases involved in chlorophyll catabolism in plants. To test the catalytic activities of these putative enzymes, representative HY2-related genes from each class were amplified by the polymerase chain reaction and expressed in Escherichia coli. Using a coupled apophytochrome assembly assay and HPLC analysis, we examined the ability of the recombinant proteins to catalyze the ferredoxin-dependent reduction of BV to phytobilins. These investigations defined three new classes of bilin reductases with distinct substrate/product specificities that are involved in the biosynthesis of the phycobiliprotein chromophore precursors phycoerythrobilin and phycocyanobilin. Implications of these results are discussed with regard to the pathways of phytobilin biosynthesis and their evolution. << Less
Plant Cell 13:965-978(2001) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.