TY - JOUR
T1 - The enzymatic biotinylation of proteins
T2 - A post-translational modification of exceptional specificity
AU - Chapman-Smith, Anne
AU - Cronan, John E.
PY - 1999/9/1
Y1 - 1999/9/1
N2 - Biotin is a coenzyme essential to all life forms. The vitamin has biological activity only when covalently attached to certain key metabolic enzymes. Most organisms have only one enzyme for attachment of biotin to other proteins and the sequences of these proteins and their substrate proteins are strongly conserved throughout nature. Structures of both the biotin ligase and the biotin carrier protein domain from Escherichia coli have been determined. These, together with mutational analyses of biotinylated proteins, are beginning to elucidate the exceptional specificity of this protein modification. Copyright (C) 1999 Elsevier Science Ltd.
AB - Biotin is a coenzyme essential to all life forms. The vitamin has biological activity only when covalently attached to certain key metabolic enzymes. Most organisms have only one enzyme for attachment of biotin to other proteins and the sequences of these proteins and their substrate proteins are strongly conserved throughout nature. Structures of both the biotin ligase and the biotin carrier protein domain from Escherichia coli have been determined. These, together with mutational analyses of biotinylated proteins, are beginning to elucidate the exceptional specificity of this protein modification. Copyright (C) 1999 Elsevier Science Ltd.
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U2 - 10.1016/S0968-0004(99)01438-3
DO - 10.1016/S0968-0004(99)01438-3
M3 - Review article
C2 - 10470036
AN - SCOPUS:0033199782
SN - 0968-0004
VL - 24
SP - 359
EP - 363
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 9
ER -