827021-73-8

Basic information

• Product Name: N^(α)-benzyloxycarbonyl-N^(ε)-9-fluorenylmethyloxycarbonyl-L-lysine benzyl ester
• Synonyms: N^(α)-benzyloxycarbonyl-N^(ε)-9-fluorenylmethyloxycarbonyl-L-lysine benzyl ester
• CAS NO: 827021-73-8
• Molecular Weight: 592.692
• Mol File: 827021-73-8.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: N^(α)-benzyloxycarbonyl-N^(ε)-9-fluorenylmethyloxycarbonyl-L-lysine benzyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N^(α)-benzyloxycarbonyl-N^(ε)-9-fluorenylmethyloxycarbonyl-L-lysine benzyl ester(827021-73-8)
• EPA Substance Registry System: N^(α)-benzyloxycarbonyl-N^(ε)-9-fluorenylmethyloxycarbonyl-L-lysine benzyl ester(827021-73-8)

Safety Data

• Hazardous Substances Data: 827021-73-8(Hazardous Substances Data)

Upstream product

• 100-39-0 benzyl bromide 
• 105751-18-6 N_α-carbobenzyloxy-N_ε-9-fluorenylmethoxycarbonyl-L-lysine 

Downstream Products

• 827021-74-9 N^(α)-benzyloxycarbonyl-N^(ε)-5-(dimethylamino)naphthalene-1-sulfonyl-L-lysine benzyl ester 
• 1101-84-4 N^(ε)-5-(dimethylamino)naphthalene-1-sulfonyl-L-lysine 
• 5591-94-6 N^(α)-benzyloxycarbonyl-L-lysine benzyl ester 

Relevant articles and documents

Synthesis of fluorescently labeled mono- and diprenylated Rab7 GTPase

Modification of proteins with isoprenoid lipids is a widespread phenomenon in eukaryotic organisms that has received much attention due to its involvement in the progression of several diseases including cancer. Progress in studies of prenylated proteins has been hampered by difficulties associated with isolation of these proteins from native or recombinant sources. Small GTPases of the Rab family represent a particularly difficult example since they are doubly C-terminally geranylgeranylated and in some cases methylated. Here, we report an efficient and versatile strategy for the synthesis of mono- and digeranylgeranylated fluorescent RabGTPases using a combination of chemical synthesis and expressed protein ligation. Using this approach we generated fluorescent mono- and diprenylated Rab7 proteins that display near-native properties and form stoichiometric complexes with their natural chaperone REP-1. We demonstrate that the complex formed from semisynthetic monoprenylated Rab7 and REP-1 represents a genuine intermediate of the Rab prenylation reaction and thus provides a unique tool for studies of the Rab prenylation mechanism. Semisynthetic Rab7 proteins were used to develop a novel fluorescence-based in vitro prenylation assay. Using this assay we dissected the mechanism of the Rab7 double-geranylgeranylation reaction mediated by Rab geranylgeranyl transferase. We conclude that the reaction follows a random sequential mechanism. These results highlight the usefulness of the semisynthetic reaction intermediates in the study of protein posttranslational modification.