Insights into Phycoerythrobilin Biosynthesis Point toward Metabolic Channeling

Dammeyer, Thorben; Frankenberg‐Dinkel, Nicole

doi:10.1074/jbc.m605154200

Cited by 56 publications

(84 citation statements)

References 30 publications

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“…PebA from cyanobacteria is thought to transfer the intermediate DHBV to PebB without releasing it to the solvent via metabolic channeling (21). As no active PebA-like enzyme from G. theta was available, PebA from Synechococcus sp.…”

Section: Resultsmentioning

confidence: 99%

“…PEB was extracted using a Sep-Pak Plus C18 cartridge, concentrated, and dried with help of a SpeedVac concentrator. The isolated PEB/isomer mixture was analyzed and separated into 3(E)-and 3(Z)-PEB via HPLC using a Ultracarb 5 ODS C18 column (Phenomenex) as described previously (21). Separated 3(E)-and 3(Z)-PEB fractions were collected, pooled, evaporated until dryness with a SpeedVac concentrator, and stored at Ϫ20°C.…”

Section: Methodsmentioning

confidence: 99%

“…The preparative production of DHBV was performed in vitro under anaerobic conditions as described before (21,35,36). 3(E)-PCB was isolated from Spirulina cells as described previously (37).…”

Section: Methodsmentioning

confidence: 99%

“…Further reduction of BV obtaining PCB, PEB, and phytochromobilin (P⌽B) is catalyzed by ferredoxin-dependent bilin reductases (FDBR) (16,19,20). In cyanobacteria, PEB biosynthesis is performed by 15,16-DHBV:ferredoxin oxidoreductase (PebA) converting BV IX␣ to the intermediate DHBV, which is subsequently reduced to PEB by the second FDBR PEB:ferredoxin oxidoreductase (PebB) (16,21). Interestingly, PebS from the cyanophage P-SSM2 is capable of performing a four-electron reduction of BV IX␣, directly yielding PEB (20).…”

mentioning

confidence: 99%

“…Pigments were extracted using a Sep-Pak Light C18 cartridge, concentrated, and dried with help of a SpeedVac concentrator. The isolated phycobilins were analyzed via HPLC as described previously (21).…”

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confidence: 99%

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Insights into the Biosynthesis and Assembly of Cryptophycean Phycobiliproteins

Overkamp

Gasper

Kock

et al. 2014

Journal of Biological Chemistry

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Background: Cryptophytes like Guillardia theta utilize soluble phycobiliproteins for light-harvesting. Results: Guillardia theta adopted phycoerythrobilin biosynthesis from cyanobacteria, and the phycobiliprotein lyase GtCPES provides structural requirements for transfer of this chromophore to a specific cysteine residue of the apophycobiliprotein. Conclusion: Phycobiliprotein synthesis in Guillardia theta combines proven and novel components. Significance: Results provide a better understanding of the evolution and function of unusual phycobiliproteins in cryptophytes.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Insights into the Biosynthesis and Assembly of Cryptophycean Phycobiliproteins

Overkamp

Gasper

Kock

et al. 2014

Journal of Biological Chemistry

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Bilin Metabolism in Plants: Structure, Function and Haem Oxygenase Regulation of Bilin Biosynthesis

Shekhawat

Parihar

Mahawar

et al. 2019

Encyclopedia of Life Sciences

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Bilins are open‐chain tetrapyrroles with a wide range of visible and nearly visible‐light absorption and emission properties. The linear tetrapyrrole molecules function as chromophores of the light‐harvesting phycobiliproteins and phytochrome‐mediated light sensing in photosynthetic organisms. They are derived from the cyclic precursor haem. The initial step in bilin biosynthesis is the conversion of haem into biliverdin (BV IX α) catalysed by haem oxygenase, which is subsequently reduced to specific bilins by ferredoxin‐dependent bilin reductases (FDBRs). Bilins usually bound to apoproteins via single or double covalent bonds to form a macromolecular complex phycobilisomes. The attachment of apoproteins to bilin is an autocatalytic process, but bilin lyases are required for the specific attachment of bilin chromophores to phycobiliprotein apoproteins. Besides the biosynthesis, structure and functions of bilins, this article also aims to recapitulate and discuss the current progress in the field of bilins and to emphasise the emerging areas. Key Concepts Bilins are open‐chain tetrapyrrole non‐metallic colour compounds formed as a metabolic product of protoporphyrin IX. Biliverdin IX α is the common precursor of all naturally occurring bilins. Haem oxygenase (HO) and ferredoxin‐dependent bilin reductases (FDBRs) are the two key enzymes involved in the biosynthesis of bilins. Phycobiliproteins assemble with bilins to form phycobilisomes, which help in light harvesting and energy transfer. Bilin plays a significant role in various physiological processes, namely, photosynthesis, respiration, light perception, signalling, cell defence against oxidative stress, nitrate and sulfate assimilation and programmed cell death.

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How to Produce a Chemical Defense: Structural Elucidation and Anatomical Distribution of Aplysioviolin and Phycoerythrobilin in the Sea Hare Aplysia californica

Kamio

Nguyen

Yaldiz

et al. 2010

Chemistry & Biodiversity

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We previously used bioassay-guided fractionation to identify phycoerythrobilin (1) and its monomethyl ester, aplysioviolin (2), as components in the ink secretion of a marine gastropod, the sea hare Aplysia californica, that act as chemical deterrents against predatory blue crabs. This was the first report of 1 as a natural product. Compound 2 was previously reported as a natural product from three species of Aplysia (A. fasciata, A. dactylomela, and A. parvula), but the reported structure and composition of stereoisomers of 2 are different among these species. Sea hares are thought to produce 2 from phycoerythrin, a photosynthetic pigment in their red-algal diet composed of a phycobiliprotein covalently linked to the chromophore 1, by cleavage of the covalent bond and methylation of 1, but neither the sequence nor the anatomical location of the cleavage and methylation is known. In this study, we clarify the structure of 1 and 2 in ink secretion of A. californica, and describe the distribution of 1 and 2 in the tissues of sea hares. We conclude that cleavage of the covalent bond in phycoerythrin occurs first, forming 1 in the digestive gland, followed by methylation of 1 to yield 2 in the ink gland.

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Insights into Phycoerythrobilin Biosynthesis Point toward Metabolic Channeling

Cited by 56 publications

References 30 publications

Insights into the Biosynthesis and Assembly of Cryptophycean Phycobiliproteins

Insights into the Biosynthesis and Assembly of Cryptophycean Phycobiliproteins

Bilin Metabolism in Plants: Structure, Function and Haem Oxygenase Regulation of Bilin Biosynthesis

How to Produce a Chemical Defense: Structural Elucidation and Anatomical Distribution of Aplysioviolin and Phycoerythrobilin in the Sea Hare Aplysia californica

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