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Substrate specificity of archaeon Sulfolobus tokodaii biotin protein ligase.

Abstract：

:Biotin protein ligase (BPL) is an enzyme mediating biotinylation of a specific lysine residue of the carboxyl carrier protein (BCCP) of biotin-dependent enzymes. We recently found that the substrate specificity of BPL from archaeon Sulfolobus tokodaii is totally different from those of many other organisms, in reflection of a difference in the local sequence of BCCP surrounding the canonical lysine residue. There is a conserved glycine residue in the biotin-binding site of Escherichia coli BPL, but this residue is replaced with alanine in S. tokodaii BPL. To test the notion that this substitution dictates the substrate specificity of the latter enzyme, this residue, Ala-43, was converted to glycine. The K(m) values of the resulting mutant, A43G, for substrates, were smaller than those of the wild type, suggesting that the residue in position 43 of BPL plays an important role in substrate binding.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sueda S,Li YQ,Kondo H,Kawarabayasi Y

doi

10.1016/j.bbrc.2006.03.118

subject

Has Abstract

pub_date

2006-05-26 00:00:00

pages

155-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00671-1

journal_volume

344

pub_type

杂志文章

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