Enzymes
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- Name help_outline all-trans-8'-apo-β-carotenal Identifier CHEBI:53154 (Beilstein: 2064131; CAS: 1107-26-2) help_outline Charge 0 Formula C30H40O InChIKeyhelp_outline DFMMVLFMMAQXHZ-DOKBYWHISA-N SMILEShelp_outline [H]C(=O)C(\C)=C\C=C\C(C)=C\C=C\C=C(C)\C=C\C=C(C)\C=C\C1=C(C)CCCC1(C)C 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
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,709 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial Identifier CHEBI:53155 Charge 0 Formula C10H12O2 InChIKeyhelp_outline PPJGVKZRXCHMCC-LNFQZQFXSA-N SMILEShelp_outline [H]C(=O)\C=C(C)\C=C\C=C(/C)C([H])=O 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
- Name help_outline all-trans-retinal Identifier CHEBI:17898 (CAS: 116-31-4) help_outline Charge 0 Formula C20H28O InChIKeyhelp_outline NCYCYZXNIZJOKI-OVSJKPMPSA-N SMILEShelp_outline [H]C(=O)\C=C(/C)\C=C\C=C(/C)\C=C\C1=C(C)CCCC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:26385 | RHEA:26386 | RHEA:26387 | RHEA:26388 | |
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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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The structure of a retinal-forming carotenoid oxygenase.
Kloer D.P., Ruch S., Al-Babili S., Beyer P., Schulz G.E.
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered ... >> More
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen. << Less
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Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803.
Ruch S., Beyer P., Ernst H., Al-Babili S.
Retinal and its derivatives represent essential compounds in many biological systems. In animals, they are synthesized through a symmetrical cleavage of beta-carotene catalysed by a monooxygenase. Here, we demonstrate that the open reading frame sll1541 from the cyanobacterium Synechocystis sp. PC ... >> More
Retinal and its derivatives represent essential compounds in many biological systems. In animals, they are synthesized through a symmetrical cleavage of beta-carotene catalysed by a monooxygenase. Here, we demonstrate that the open reading frame sll1541 from the cyanobacterium Synechocystis sp. PCC 6803 encodes the first eubacterial, retinal synthesizing enzyme (Diox1) thus far reported. In contrast to enzymes from animals, Diox1 converts beta-apo-carotenals instead of beta-carotene into retinal in vitro. The identity of the enzymatic product was proven by HPLC, GC-MS and in a biological test. Investigations, of the stereospecifity showed that Diox1 cleaved only the all-trans form of beta-apo-8'-carotenal, yielding all-trans-retinal. However, Diox1 exhibited wide substrate specificity with respect to chain-lengths and functional end-groups. Although with divergent Km and Vmax values, the enzyme converted beta-apo-carotenals, (3R)-3-OH-beta-apo-carotenals as well as apo-lycopenals into retinal, (3R)-3-hydroxy-retinal and acycloretinal respectively. In addition, the alcohols of these substrates were cleaved to yield the corresponding retinal derivatives. << Less
Mol. Microbiol. 55:1015-1024(2005) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.