Is anyone aware of a good proteomic study aimed at identifying endogenously biotinylated proteins? I know that a handful of mitochondrial proteins are known to have biotin cofactors, but wondered if anyone has done a proteome-wide MS-based study to identify endogenously biotinylated proteins in an unbiased way. Thanks.
That is not biotinylation, but the transfer of biotin onto the epsilon-amino group of Lys (biocytin formation) in enzymes that have biotin as permanently bound cofactor (prosthetic group). Cannonically, those are carboxylases (E.C. 6.4.1.x). Consult a standard textbook of biochemistry for more details.
Hmmmm. I'm confused. I'm operating under the following definition of biotinylation:
"In biochemistry, biotinylation is the process of covalently attaching biotin to a protein, nucleic acid or other molecule." (https://en.wikipedia.org/wiki/Biotinylation)
I'll look into biocytin and it's contrast to biotinylation.
Anyway, my question still remains: Has anyone done an unbiased proteome-wide proteomic study trying to identify proteins covalently modified by biotin? Forgive me if I've used the incorrect terminology, but I hope the request is clear.
As I said I am aware of the canonical substrates/targets/acceptors.
As far as I can see biocytin is the name of a specific biotin-lysine amide compound with chemical formula C16H28N4O4S, Molar mass = 372.48 g·mol−1 (https://en.wikipedia.org/wiki/Biocytin). It seems to be a specific chemical and not a post-translational protein modification. Although I'd happily read further if you can give me a good ref. Chemistry is not my forte.
I'm still interested an any answers to the original question.
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