A mechanism-based cross-linker for the identification of kinase-substrate pairs

Journal of the American Chemical Society

Volumn 126, Issue 30, 2004, Pages 9160-9161

  Maly, Dustin J ^a   Allen, Jasmina A ^a   Shokat, Kevan M ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING SITE; COVALENT BOND; CROSS LINKING; ENZYME DENATURATION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE COMPLEX; REACTION ANALYSIS;

ADENOSINE; ADENOSINE TRIPHOSPHATE; BINDING SITES; CROSS-LINKING REAGENTS; CYSTEINE; O-PHTHALALDEHYDE; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN-SERINE-THREONINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-AKT; SERINE; SUBSTRATE SPECIFICITY; THREONINE;

EID: 3342931068     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja048659i     Document Type: Article

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17. Under the reaction conditions described in Figure 2A, 20-25% of the kinase is cross-linked to the peptide substrate (Supporting Information, Figure 1). For an analysis of the kinetics of the cross-linking reaction see Supporting Information, Figure 2.