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B6db references: 15689518

type Journal Article
authors Sun L, Bartlam M, Liu Y, Pang H, Rao Z.
title Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver
journal Acta Crystallogr D Biol Crystallogr
sel selected
ui 15689518
year (2005)
volume 14
number 3
pages 791-8
abstract L-serine dehydratase (SDH), a member of the beta-family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or 2-oxobutyrate. The crystal structure of L-serine dehydratase from human liver (hSDH) has been solved at 2.5 A-resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for beta-family PLP-dependent enzymes. Each monomer serves as an active unit and is subdivided into two distinct domains: a small domain and a PLP-binding domain that covalently anchors the cofactor. Both domains show the typical open alpha/beta architecture of PLP enzymes. Comparison with the rSDH-(PLP-OMS) holo-enzyme reveals a large structural difference in active sites caused by the artifical O-methylserine. Furthermore, the activity of hSDH-PLP was assayed and it proved to show catalytic activity. That suggests that the structure of hSDH-PLP is the first structure of the active natural holo-SDH.
last changed 2008/03/27 19:30

B6db references