Quo vadis photorespiration: A tale of two aldolases

被引:27
作者
Hixon, M
Sinerius, G
Schneider, A
Walter, C
Fessner, WD
Schloss, JV
机构
[1] UNIV KANSAS,DEPT MED CHEM,LAWRENCE,KS 66045
[2] RHEIN WESTFAL TH AACHEN,INST ORGAN CHEM,D-52056 AACHEN,GERMANY
关键词
D-ribulose 1,5-bisphosphate carboxylase/oxygenase; photorespiration; L-rhamnulose I-phosphate aldolase; L-fuculose l-phosphate aldolase; ene-diol; oxygenase;
D O I
10.1016/0014-5793(96)00830-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 l-phosphate aldolase and L-fuculose l-phosphate aldolase, The former enzyme has an oxygenase activity, while the latter does not, suggesting that the reaction with O-2 is not inevitable.
引用
收藏
页码:281 / 284
页数:4
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