Identification of Lys190 as the primary binding site for pyridoxal 5'-phosphate in human serum albumin.

Abstract:

:The covalent binding of pyridoxal 5'-phosphate (PLP) to human serum albumin (HSA) is important in the regulation of PLP metabolism. In plasma, PLP is bound to HSA at a single high-affinity and at two or more nonspecific sites. To characterize the primary PLP binding site, HSA was incubated with [3H] PLP, and the Schiff base linkage was reduced with potassium borohydride. Tryptic peptides were purified, and the major labeled peptide was sequenced. Amino acid analysis confirmed a homogeneous peptide Leu-Asp-Glu-Leu-Arg-Asp-Glu-Gly-Xaa-Ala-Ser-Ser-Ala-Lys which corresponds to residues 182-195 of HSA. The data indicate that Lys190 is the primary PLP binding site. This Lys residue is distinct from other sites of covalent adduct formation; namely, the primary sites for nonenzymatic glycosylation (Lys525) and acetylation by aspirin (Lys199).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bohney JP,Fonda ML,Feldhoff RC

doi

10.1016/0014-5793(92)80073-p

keywords:

subject

Has Abstract

pub_date

1992-02-24 00:00:00

pages

266-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80073-P

journal_volume

298

pub_type

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