STUDIES ON CHLOROPHYLLASE OF &lt;italic&gt;CHLORELLA PROTOTHECOIDES&lt;/italic&gt;I. ENZYMATIC PHYTYLATION OF METHYL CHLOROPHYLLIDE&lt;xref ref-type="fn" rid="fn1"&gt;&lt;sup&gt;1&lt;/sup&gt;&lt;/xref&gt;

Chiba, Yasutane; Aiga, Ichiro; Idemori, Masahiro; Satoh, Yoko; Matsushita, Kamehisa; Sasa, Tsutomu

doi:10.1093/oxfordjournals.pcp.a079298

Cited by 4 publications

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“…Over the following years, examination of the in vitro esterification activity of algal and plant chlorophyllases produced conflicting results [23][24][25][26]. Although chlorophyllase appeared capable of esterifying various species of Chlide with differing tetraprenyl moieties [27,28], the enzyme invariably demonstrated a requirement for high concentrations of Chlide biosynthesis are shared between all photosynthetic organisms and involve chelation of a magnesium ion at the centre of the porphyrin ring and formation of the characteristic ring E producing divinyl-protochlorophyllide a (DV-PChlide a). Reduction of ring D of DV-PChlide a produces divinyl-chlorophyllide a, the last common precursor in plants, algae Ã and cyanobacteria, purple bacteria, heliobacteria, and 'green bacteria' (green sulfur bacteria, filamentous anoxygenic phototrophs (FAPs) and Acidobacteria).…”

Section: Discovery Of (Bacterio)chlorophyll Synthases In Photosynthet...mentioning

confidence: 99%

The terminal enzymes of (bacterio)chlorophyll biosynthesis

et al. 2022

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(Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.

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