Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Hu IC
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------>journal_name=Biochemistry
------>paper_name=Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalytic bilin attachment.
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------>fullAbstract=Allophycocyanin (APC) is one of the phycobiliproteins expressed in cyanobacteria. Phycobiliproteins contain a covalently bound chromophore, and thus, they are valuable as fluorescent probes. Biosynthesis of a functional phycobiliprotein is achieved by a bilin attachment process between the chromophore and apoprotein. Chromophore lyases are necessary to catalyze the chromophorylation of cyanobacterial phycobiliproteins, such as C-phycocyanin, and phycoerythrocyanin. To identify the lyase that catalyzes the chromophorylation of the APC alpha-subunit (ApcA), we searched the entire genomes of two cyanobacteria, Synechocystis sp. PCC6803 and Anabaena sp. PCC 7120; however, these genomes do not appear to encode an APC-specific chromophore lyase. In this study, chromophorylated ApcA (chromo-ApcA) was obtained via a spontaneous bilin attachment reaction. The absorption and fluorescence characteristics of chromo-ApcA were similar to those of the native APC alpha-subunit. The extent of chromophore attachment to apo-ApcA was comparable to that of the lyase-catalyzed reactions for other phycobiliproteins. These results indicate that ApcA has autocatalytic bilin:biliprotein lyase activity.
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------>authors2=Lee TR
------>authors3=Lin HF
------>authors4=Chiueh CC
------>authors5=Lyu PC
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------>authors=Hu IC
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------>updateTitle=Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalytic bilin attachment.
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------>no=23
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------>publish_year=2006
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------>publish_month=6
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z