1FDZ

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION

1FDZ の概要

• エントリーDOI: 10.2210/pdb1fdz/pdb
• 分子名称: N-ACETYLNEURAMINATE LYASE, PYRUVIC ACID (3 entities in total)
• 機能のキーワード: lyase, aldolase, oxo-acid lyase, alpha-keto-acid lyase, carbon-carbon lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6L4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130857.75

構造登録者

Lawrence, M.C.,Barbosa, J.A.R.G.,Smith, B.J.,Hall, N.E.,Pilling, P.A.,Ooi, H.C.,Marcuccio, S.M. (登録日: 1996-07-08, 公開日: 1997-10-22, 最終更新日: 2024-10-16)

主引用文献

Lawrence, M.C.,Barbosa, J.A.R.G.,Smith, B.J.,Hall, N.E.,Pilling, P.A.,Ooi, H.C.,Marcuccio, S.M.
Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
J.Mol.Biol., 266:381-399, 1997

PubMed Abstract: We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear.

PubMed: 9047371
DOI: 10.1006/jmbi.1996.0769

実験手法

X-RAY DIFFRACTION (2.6 Å)