Quo vadis photorespiration: A tale of two aldolases
An O 2-consuming side reaction of d-ribulose 1,5-bisphosphate carboxylase causes photorespiration in plants. This reaction may be an inevitable consequence of the enzyme's inability to protect its ene-diolate reaction intermediate from O 2, a notion that is supported by the failure of persisten...
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Veröffentlicht in: | FEBS letters 1996-09, Vol.392 (3), p.281-284 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | An O
2-consuming side reaction of
d-ribulose 1,5-bisphosphate carboxylase causes photorespiration in plants. This reaction may be an inevitable consequence of the enzyme's inability to protect its ene-diolate reaction intermediate from O
2, a notion that is supported by the failure of persistent efforts to eliminate selectively its oxygenase activity by genetic manipulation. We have examined two aldolases with similar ene-diolate intermediates,
l-rhamnulose 1-phosphate aldolase and
l-fuculose 1-phosphate aldolase. The former enzyme has an oxygenase activity, while the latter does not, suggesting that the reaction with O
2 is not inevitable. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(96)00830-7 |